Journal articles: 'Non histone protein'

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Al-Hamashi, Ayad A., Krystal Diaz, and Rong Huang. "Non-Histone Arginine Methylation by Protein Arginine Methyltransferases." Current Protein & Peptide Science 21, no. 7 (September 23, 2020): 699–712. http://dx.doi.org/10.2174/1389203721666200507091952.

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Protein arginine methyltransferase (PRMT) enzymes play a crucial role in RNA splicing, DNA damage repair, cell signaling, and differentiation. Arginine methylation is a prominent posttransitional modification of histones and various non-histone proteins that can either activate or repress gene expression. The aberrant expression of PRMTs has been linked to multiple abnormalities, notably cancer. Herein, we review a number of non-histone protein substrates for all nine members of human PRMTs and how PRMT-mediated non-histone arginine methylation modulates various diseases. Additionally, we highlight the most recent clinical studies for several PRMT inhibitors.

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Kumar, Amish, and Gitanjali Yadav. "Shared ancestry of core-histone subunits and non-histone plant proteins containing the Histone Fold Motif (HFM)." Journal of Bioinformatics and Computational Biology 19, no. 02 (April 2021): 2140001. http://dx.doi.org/10.1142/s0219720021400011.

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The three helical Histone Fold Motif (HFM) of core histone proteins provides an evolutionarily favored site for the protein–DNA interface. Despite significant variation in sequence, the HFM retains a distinctive structural fold that has diversified into several non-histone protein families. In this work, we explore the ancestry of non-histone HFM containing families in the plant kingdom. A sequence search algorithm was developed using iterative profile Hidden Markov Models to identify remote homologs of core-histone proteins. The resulting hits were functionally annotated, classified into families, and subjected to comprehensive phylogenetic analyses via Maximum likelihood and Bayesian methods. We have identified 4390 HFM containing proteins in the plant kingdom that are not histones, mostly existing as diverse transcription factor families, distributed widely within and across taxonomic groups. Patterns of homology suggest that core histone subunit H2A has evolved into newer families like NF-YC and DRAP1, whereas the H2B subunit of core histones shares a common ancestry with NF-YB and DR1 class of TFs. Core histone subunits H3 and H4 were found to have evolved into DPE and TAF proteins, respectively. Taken together these results provide insights into diversification events during the evolution of the HFM, including sub-functionalization and neo-functionalization of the HFM.

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Traub, Peter, Georg Perides, Siegfried Kühn, and Annemarie Scherbarth. "Interaction in vitro of Non-Epithelial Intermediate Filament Proteins with Histones." Zeitschrift für Naturforschung C 42, no. 1-2 (February 1, 1987): 47–63. http://dx.doi.org/10.1515/znc-1987-1-209.

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Abstract Non-epithelial intermediate filament (IF) subunit proteins show a high and specific affinity for core histones at physiological ionic strength. When IF proteins are titrated with a mixture of core histones and linker histone H1, in general the latter is totally excluded from com plexation and in the adducts formed the moderately-arginine-rich histones H2A and H2B are progressively replaced by the very-arginine-rich histones H3 and H4. At histone saturation, 2 molecules of nonneuronal IF protein bind 1 histone HI molecule or 8 core histone m olecules, whereas due to its glutamic acid rich, C terminal extensions one dimer of thp 68 kD npnrofilament nrotein associates with 3 molecules of histone H1 or 24 molecules of core histones. The salt stability of the insoluble association products is dependent on the amount and arginine content of the constituent histone species. Rem oval of the non-α-helical N- and C-terminal polypeptides from IF proteins by partial chymotryptic digestion does not affect their histone-binding characteristics. Since core histones are only partially inactivated by limited tryptic digestion, they also appear to react through their a-helix-rich central domains; the limit peptide derived from histone H1 is com pletely inactive at physiological ionic strength. Affinity chromatography of rod domains of IF proteins on core histone-Sepharose 4B and of histones and their limit peptides on vim entin-Sepharose 4B has shown that the interactions involving fractions of histones H3 and H4 are extrem ely resistant to salt and can be dissociated only with arginine or salt under denaturing conditions. In general, the experim ental results revealed close parallels between the association of histones with IF proteins and their interaction with DNA.

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Fonin, Alexander V., Olga V. Stepanenko, Irina M. Kuznetsova, Konstantin K. Turoverov, Elena I. Kostyleva, and Vladimir I. Vorobyev. "Interaction between linker histone H1 and non-histone chromatin protein HMGB1." Spectroscopy 24, no. 1-2 (2010): 165–68. http://dx.doi.org/10.1155/2010/745671.

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The possibility of interaction between linker histone H1 and non-histone chromatin protein HMGB1 was studied by intrinsic UV-fluorescence, far and near-UV CD and light scattering. The obtained data allow us to assume that the increase of histone H1 content in the HMGB1 solutions in a low ionic strength is accompanied by the destruction of HMGB1 associates. The interaction between proteins causes the increase of ordered regions in the protein molecules and the minor changes in their tertiary structure.

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Gong, Ping, Yuetong Wang, and Yongkui Jing. "Apoptosis Induction byHistone Deacetylase Inhibitors in Cancer Cells: Role of Ku70." International Journal of Molecular Sciences 20, no. 7 (March 30, 2019): 1601. http://dx.doi.org/10.3390/ijms20071601.

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Histone deacetylases (HDACs) are a group of enzymes that regulate gene transcription by controlling deacetylation of histones and non-histone proteins. Overexpression of HDACs is found in some types of tumors and predicts poor prognosis. Five HDAC inhibitors are approved for the treatment of cutaneous T-cell lymphoma, peripheral T-cell lymphoma, and multiple myeloma. Treatment with HDAC inhibitors regulates gene expression with increased acetylated histones with unconfirmed connection with therapy. Apoptosis is a key mechanism by which HDAC inhibitors selectively kill cancer cells, probably due to acetylation of non-histone proteins. Ku70 is a protein that repairs DNA breaks and stabilizes anti-apoptotic protein c-FLIP and proapoptotic protein Bax, which is regulated by acetylation. HDAC inhibitors induce Ku70 acetylation with repressed c-FLIP and activated Bax in cancer cells. Current studies indicate that Ku70 is a potential target of HDAC inhibitors and plays an important role during the induction of apoptosis.

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NAKAYAMA, TATSUO. "Vitellogenin-specific Non-histone Chromatin Protein. (tissue-specific gene/vitellogenin gene/non-histone chromatin protein/HPLC)." Development, Growth and Differentiation 28, no. 5 (September 1986): 425–29. http://dx.doi.org/10.1111/j.1440-169x.1986.00425.x.

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Chikhirzhina, Elena, Tatyana Starkova, Anton Beljajev, Alexander Polyanichko, and Alexey Tomilin. "Functional Diversity of Non-Histone Chromosomal Protein HmgB1." International Journal of Molecular Sciences 21, no. 21 (October 26, 2020): 7948. http://dx.doi.org/10.3390/ijms21217948.

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The functioning of DNA in the cell nucleus is ensured by a multitude of proteins, whose interactions with DNA as well as with other proteins lead to the formation of a complicated, organized, and quite dynamic system known as chromatin. This review is devoted to the description of properties and structure of the progenitors of the most abundant non-histone protein of the HMGB family—the HmgB1 protein. The proteins of the HMGB family are also known as “architectural factors” of chromatin, which play an important role in gene expression, transcription, DNA replication, and repair. However, as soon as HmgB1 goes outside the nucleus, it acquires completely different functions, post-translational modifications, and change of its redox state. Despite a lot of evidence of the functional activity of HmgB1, there are still many issues to be solved related to the mechanisms of the influence of HmgB1 on the development and treatment of different diseases—from oncological and cardiovascular diseases to pathologies during pregnancy and childbirth. Here, we describe molecular structure of the HmgB1 protein and discuss general mechanisms of its interactions with other proteins and DNA in cell.

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Li, Hong-Tao, Ting Gong, Zhen Zhou, Yu-Ting Liu, Xiongwen Cao, Yongning He, Charlie Degui Chen, and Jin-Qiu Zhou. "Yeast Hmt1 catalyses asymmetric dimethylation of histone H3 arginine 2 in vitro." Biochemical Journal 467, no. 3 (April 17, 2015): 507–15. http://dx.doi.org/10.1042/bj20141437.

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Protein arginine methyltransferases (PRMTs) are a family of enzymes that can methylate protein arginine residues. PRMTs’ substrates include histones and a variety of non-histone proteins. Previous studies have shown that yeast Hmt1 is a type I PRMT and methylates histone H4 arginine 3 and several mRNA-binding proteins. Hmt1 forms dimers or oligomers, but how dimerization or oligomerization affects its activity remains largely unknown. We now report that Hmt1 can methylate histone H3 arginine 2 (H3R2) in vitro. The dimerization but not hexamerization is essential for Hmt1’s activity. Interestingly, the methyltransferase activity of Hmt1 on histone H3R2 requires reciprocal contributions from two Hmt1 molecules. Our results suggest an intermolecular trans-complementary mechanism by which Hmt1 dimer methylates its substrates.

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Habibian, Justine, and Bradley Ferguson. "The Crosstalk between Acetylation and Phosphorylation: Emerging New Roles for HDAC Inhibitors in the Heart." International Journal of Molecular Sciences 20, no. 1 (December 28, 2018): 102. http://dx.doi.org/10.3390/ijms20010102.

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Approximately five million United States (U.S.) adults are diagnosed with heart failure (HF), with eight million U.S. adults projected to suffer from HF by 2030. With five-year mortality rates following HF diagnosis approximating 50%, novel therapeutic treatments are needed for HF patients. Pre-clinical animal models of HF have highlighted histone deacetylase (HDAC) inhibitors as efficacious therapeutics that can stop and potentially reverse cardiac remodeling and dysfunction linked with HF development. HDACs remove acetyl groups from nucleosomal histones, altering DNA-histone protein electrostatic interactions in the regulation of gene expression. However, HDACs also remove acetyl groups from non-histone proteins in various tissues. Changes in histone and non-histone protein acetylation plays a key role in protein structure and function that can alter other post translational modifications (PTMs), including protein phosphorylation. Protein phosphorylation is a well described PTM that is important for cardiac signal transduction, protein activity and gene expression, yet the functional role for acetylation-phosphorylation cross-talk in the myocardium remains less clear. This review will focus on the regulation and function for acetylation-phosphorylation cross-talk in the heart, with a focus on the role for HDACs and HDAC inhibitors as regulators of acetyl-phosphorylation cross-talk in the control of cardiac function.

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Xu, Qiutao, Qian Liu, Zhengting Chen, Yaping Yue, Yuan Liu, Yu Zhao, and Dao-Xiu Zhou. "Histone deacetylases control lysine acetylation of ribosomal proteins in rice." Nucleic Acids Research 49, no. 8 (April 9, 2021): 4613–28. http://dx.doi.org/10.1093/nar/gkab244.

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Abstract Lysine acetylation (Kac) is well known to occur in histones for chromatin function and epigenetic regulation. In addition to histones, Kac is also detected in a large number of proteins with diverse biological functions. However, Kac function and regulatory mechanism for most proteins are unclear. In this work, we studied mutation effects of rice genes encoding cytoplasm-localized histone deacetylases (HDAC) on protein acetylome and found that the HDAC protein HDA714 was a major deacetylase of the rice non-histone proteins including many ribosomal proteins (r-proteins) and translation factors that were extensively acetylated. HDA714 loss-of-function mutations increased Kac levels but reduced abundance of r-proteins. In vitro and in vivo experiments showed that HDA714 interacted with r-proteins and reduced their Kac. Substitutions of lysine by arginine (depleting Kac) in several r-proteins enhance, while mutations of lysine to glutamine (mimicking Kac) decrease their stability in transient expression system. Ribo-seq analysis revealed that the hda714 mutations resulted in increased ribosome stalling frequency. Collectively, the results uncover Kac as a functional posttranslational modification of r-proteins which is controlled by histone deacetylases, extending the role of Kac in gene expression to protein translational regulation.

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Fonin, A. V., Olga V. Stepanenko, K. K. Turoverov, and V. I. Vorobyev. "Interaction between non-histone chromatin protein HMGB1 and linker histone H1." Cell and Tissue Biology 5, no. 2 (April 2011): 120–22. http://dx.doi.org/10.1134/s1990519x11020076.

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Bertos, Nicholas R., Audrey H. Wang, and Xiang-Jiao Yang. "Class II histone deacetylases: Structure, function, and regulation." Biochemistry and Cell Biology 79, no. 3 (June 1, 2001): 243–52. http://dx.doi.org/10.1139/o01-032.

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Acetylation of histones, as well as non-histone proteins, plays important roles in regulating various cellular processes. Dynamic control of protein acetylation levels in vivo occurs through the opposing actions of histone acetyltransferases and histone deacetylases (HDACs). In the past few years, distinct classes of HDACs have been identified in mammalian cells. Class I members, such as HDAC1, HDAC2, HDAC3, and HDAC8, are well-known enzymatic transcriptional corepressors homologous to yeast Rpd3. Class II members, including HDAC4, HDAC5, HDAC6, HDAC7, and HDAC9, possess domains similar to the deacetylase domain of yeast Hda1. HDAC4, HDAC5, and HDAC7 function as transcriptional corepressors that interact with the MEF2 transcription factors and the N-CoR, BCoR, and CtBP corepressors. Intriguingly, HDAC4, HDAC5, and probably HDAC7 are regulated through subcellular compartmentalization controlled by site-specific phosphorylation and binding of 14-3-3 proteins; the regulation of these HDACs is thus directly linked to cellular signaling networks. Both HDAC6 and HDAC9 possess unique structural modules, so they may have special biological functions. Comprehension of the structure, function, and regulation of class II deacetylases is important for elucidating how acetylation regulates functions of histones and other proteins in vivo.Key words: histone acetylation, protein acetylation, histone deacetylase, 14-3-3 proteins.

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Demyanenko, Svetlana, and Svetlana Sharifulina. "The Role of Post-Translational Acetylation and Deacetylation of Signaling Proteins and Transcription Factors after Cerebral Ischemia: Facts and Hypotheses." International Journal of Molecular Sciences 22, no. 15 (July 26, 2021): 7947. http://dx.doi.org/10.3390/ijms22157947.

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Histone deacetylase (HDAC) and histone acetyltransferase (HAT) regulate transcription and the most important functions of cells by acetylating/deacetylating histones and non-histone proteins. These proteins are involved in cell survival and death, replication, DNA repair, the cell cycle, and cell responses to stress and aging. HDAC/HAT balance in cells affects gene expression and cell signaling. There are very few studies on the effects of stroke on non-histone protein acetylation/deacetylation in brain cells. HDAC inhibitors have been shown to be effective in protecting the brain from ischemic damage. However, the role of different HDAC isoforms in the survival and death of brain cells after stroke is still controversial. HAT/HDAC activity depends on the acetylation site and the acetylation/deacetylation of the main proteins (c-Myc, E2F1, p53, ERK1/2, Akt) considered in this review, that are involved in the regulation of cell fate decisions. Our review aims to analyze the possible role of the acetylation/deacetylation of transcription factors and signaling proteins involved in the regulation of survival and death in cerebral ischemia.

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WONDRAK, Georg T., Daniel CERVANTES-LAUREAN, Elaine L. JACOBSON, and Myron K. JACOBSON. "Histone carbonylation in vivo and in vitro." Biochemical Journal 351, no. 3 (October 24, 2000): 769–77. http://dx.doi.org/10.1042/bj3510769.

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Non-enzymic damage to nuclear proteins has potentially severe consequences for the maintenance of genomic integrity. Introduction of carbonyl groups into histones in vivo and in vitro was assessed by Western blot immunoassay and reductive incorporation of tritium from radiolabelled NaBH4 (sodium borohydride). Histone H1 extracted from bovine thymus, liver and spleen was found to contain significantly elevated amounts of protein-bound carbonyl groups as compared with core histones. The carbonyl content of nuclear proteins of rat pheochromocytoma cells (PC12 cells) was not greatly increased following oxidative stress induced by H2O2, but was significantly increased following alkylating stress induced by N-methyl-N´-nitro-N-nitrosoguanidine or by combined oxidative and alkylating stress. Free ADP-ribose, a reducing sugar generated in the nucleus in proportion to DNA strand breaks, was shown to be a potent histone H1 carbonylating agent in isolated PC12 cell nuclei. Studies of the mechanism of histone H1 modification by ADP-ribose indicate that carbonylation involves formation of a stable acyclic ketoamine. Our results demonstrate preferential histone H1 carbonylation in vivo, with potentially important consequences for chromatin structure and function.

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Narita, Takeo, Brian T. Weinert, and Chunaram Choudhary. "Functions and mechanisms of non-histone protein acetylation." Nature Reviews Molecular Cell Biology 20, no. 3 (November 22, 2018): 156–74. http://dx.doi.org/10.1038/s41580-018-0081-3.

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Ryan, J., A. J. Llinas, D. A. White, B. M. Turner, and J. Sommerville. "Maternal histone deacetylase is accumulated in the nuclei of Xenopus oocytes as protein complexes with potential enzyme activity." Journal of Cell Science 112, no. 14 (July 15, 1999): 2441–52. http://dx.doi.org/10.1242/jcs.112.14.2441.

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Reversible acetylation of core histones plays an important regulatory role in transcription and replication of chromatin. The acetylation status of chromatin is determined by the equilibrium between activities of histone acetyltransferases (HATs) and histone deacetylases (HDACs). The Xenopus protein HDACm shows sequence homology to other putative histone deacetylases, but its mRNA is expressed only during early development. Both HDACm protein and acetylated non-chromosomal histones are accumulated in developing oocytes, indicating that the key components for histone deposition into new chromatin during blastula formation are in place by the end of oogenesis. Here we show that the 57 kDa HDACm protein undergoes steady accumulation in the nucleus, where it is organized in a multiprotein complex of approx. 300 kDa. A second, major component of the nuclear complex is the retinoblastoma-associated protein p48 (RbAp48/46), which may be used as an adaptor to contact acetylated histones in newly assembled chromatin. The nuclear complex has HDAC activity that is sensitive to trichostatin A, zinc ions and phosphatase treatment. The 57 kDa protein serves as a marker for total HDAC activity throughout oogenesis and early embryogenesis. The active HDACm complex and its acetylated histone substrates appear to be kept apart until after chromatin assembly has taken place. However, recombinant HDACm, injected into the cytoplasm of oocytes, not only is translocated to the nucleus, but also is free to interact with the endogenous chromatin.

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Mendiratta, Shweta, Alberto Gatto, and Genevieve Almouzni. "Histone supply: Multitiered regulation ensures chromatin dynamics throughout the cell cycle." Journal of Cell Biology 218, no. 1 (September 26, 2018): 39–54. http://dx.doi.org/10.1083/jcb.201807179.

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As the building blocks of chromatin, histones are central to establish and maintain particular chromatin states associated with given cell fates. Importantly, histones exist as distinct variants whose expression and incorporation into chromatin are tightly regulated during the cell cycle. During S phase, specialized replicative histone variants ensure the bulk of the chromatinization of the duplicating genome. Other non-replicative histone variants deposited throughout the cell cycle at specific loci use pathways uncoupled from DNA synthesis. Here, we review the particular dynamics of expression, cellular transit, assembly, and disassembly of replicative and non-replicative forms of the histone H3. Beyond the role of histone variants in chromatin dynamics, we review our current knowledge concerning their distinct regulation to control their expression at different levels including transcription, posttranscriptional processing, and protein stability. In light of this unique regulation, we highlight situations where perturbations in histone balance may lead to cellular dysfunction and pathologies.

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Polyanichko, Alexander, and Helmut Wieser. "Structural organization of DNA–protein complexes of chromatin studied by vibrational and electronic circular dichroism." Spectroscopy 24, no. 3-4 (2010): 239–44. http://dx.doi.org/10.1155/2010/658374.

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Structure and functioning of chromatin is determined by interactions of DNA with numerous nuclear proteins. The most abundant and yet not completely understood non-histone chromosomal proteins are those belonging to a High Mobility Group (HMG) namely HMGB1. The interplay of this protein on DNA with linker histone H1 and other proteins determines both structure and functioning of the chromatin. A combination of UV and IR absorption and circular dichroism (CD) spectroscopy was applied to investigate the structure and formation of large supramolecular DNA–protein complexes. This combination of techniques was used to overcome limitations of UV-CD (ECD) spectroscopy due to considerable light scattering in such solutions. Based on the analysis of FTIR and UV circular dichroism spectra and AFM imaging the interaction of DNA with high-mobility group non-histone chromatin protein HMGB1 and linker histone H1 was studied.

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Kohlstaedt, L. A., E. C. Sung, A. Fujishige, and R. D. Cole. "Non-histone chromosomal protein HMG1 modulates the histone H1-induced condensation of DNA." Journal of Biological Chemistry 262, no. 2 (January 1987): 524–26. http://dx.doi.org/10.1016/s0021-9258(19)75811-6.

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Khan, Ahlia N., and Peter N. Lewis. "Unstructured Conformations Are a Substrate Requirement for the Sir2 Family of NAD-dependent Protein Deacetylases." Journal of Biological Chemistry 280, no. 43 (August 29, 2005): 36073–78. http://dx.doi.org/10.1074/jbc.m508247200.

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The regulation of protein function is often achieved through post-translational modifications including phosphorylation, methylation, ubiquitination, and acetylation. The role of acetylation has been most extensively studied in the context of histones, but it is becoming increasingly evident that this modification now includes other proteins. The Sir2 family of NAD-dependent deacetylases was initially recognized as mediating gene silencing through histone deacetylation, but several family members display non-nuclear sub-cellular localization and deacetylate non-histone protein substrates. Although many structural and enzymatic studies of Sir2 proteins have been reported, how substrate recognition is achieved by this family of enzymes is unknown. Here we use in vitro deacetylase assays and a variety of potential substrates to examine the substrate specificity of yeast homologue Hst2. We show that Hst2 is specific for acetyl-lysine within proteins; it does not deacetylate small polycations such as acetyl-spermine or acetylated amino ter-mini of proteins. Furthermore we have found that Hst2 displays conformational rather than sequence specificity, preferentially deacetylating acetyl-lysine within unstructured regions of proteins. Our results suggest that this conformational requirement may be a general feature for substrate recognition in the Sir2 family.

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Wei, Han, Rasika Mundade, Kevin Lange, and Tao Lu. "Protein arginine methylation of non-histone proteins and its role in diseases." Cell Cycle 13, no. 1 (December 2, 2013): 32–41. http://dx.doi.org/10.4161/cc.27353.

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Salvi, Mauro. "Non-Histone Protein Methylation: Molecular Mechanisms and Physiopathological Relevance." Current Protein & Peptide Science 21, no. 7 (September 23, 2020): 640–41. http://dx.doi.org/10.2174/138920372107200620152550.

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Štros, Michal, and Gordon H. Dixon. "A retropseudogene for non-histone chromosomal protein HMG-1." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1172, no. 1-2 (February 1993): 231–35. http://dx.doi.org/10.1016/0167-4781(93)90303-u.

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Friedmann, David R., and Ronen Marmorstein. "Structure and mechanism of non-histone protein acetyltransferase enzymes." FEBS Journal 280, no. 22 (June 28, 2013): 5570–81. http://dx.doi.org/10.1111/febs.12373.

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Landsman, David, and Michael Bustin. "Chicken non-histone chromosomal protein HMG-17 cDNA sequence." Nucleic Acids Research 15, no. 16 (1987): 6750. http://dx.doi.org/10.1093/nar/15.16.6750.

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Rathert, Philipp, Arunkumar Dhayalan, Marie Murakami, Xing Zhang, Raluca Tamas, Renata Jurkowska, Yasuhiko Komatsu, Yoichi Shinkai, Xiaodong Cheng, and Albert Jeltsch. "Protein lysine methyltransferase G9a acts on non-histone targets." Nature Chemical Biology 4, no. 6 (April 27, 2008): 344–46. http://dx.doi.org/10.1038/nchembio.88.

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Landsman, David, and Michael Bustin. "Mouse non-histone chromosomal protein HMG-14 cDNA sequence." Nucleic Acids Research 18, no. 17 (1990): 5311. http://dx.doi.org/10.1093/nar/18.17.5311.

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Landsman, David, Stella Zavou, Nirmolini Soares, Graham H. Goodwin, and Michael Bustin. "Mouse non-histone chromosomal protein HMG-17 cDNA sequence." Nucleic Acids Research 16, no. 21 (1988): 10386. http://dx.doi.org/10.1093/nar/16.21.10386.

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Di Blasi, Roberto, Oleg Blyuss, John F. Timms, Daniel Conole, Francesca Ceroni, and Harry J. Whitwell. "Non-Histone Protein Methylation: Biological Significance and Bioengineering Potential." ACS Chemical Biology 16, no. 2 (January 7, 2021): 238–50. http://dx.doi.org/10.1021/acschembio.0c00771.

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Hard, Ryan, Nan Li, Wei He, Brian Ross, Gary C. H. Mo, Qin Peng, Richard S. L. Stein, et al. "Deciphering and engineering chromodomain-methyllysine peptide recognition." Science Advances 4, no. 11 (November 2018): eaau1447. http://dx.doi.org/10.1126/sciadv.aau1447.

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Posttranslational modifications (PTMs) play critical roles in regulating protein functions and mediating protein-protein interactions. An important PTM is lysine methylation that orchestrates chromatin modifications and regulates functions of non-histone proteins. Methyllysine peptides are bound by modular domains, of which chromodomains are representative. Here, we conducted the first large-scale study of chromodomains in the human proteome interacting with both histone and non-histone methyllysine peptides. We observed significant degenerate binding between chromodomains and histone peptides, i.e., different histone sites can be recognized by the same set of chromodomains, and different chromodomains can share similar binding profiles to individual histone sites. Such degenerate binding is not dictated by amino acid sequence or PTM motif but rather rooted in the physiochemical properties defined by the PTMs on the histone peptides. This molecular mechanism is confirmed by the accurate prediction of the binding specificity using a computational model that captures the structural and energetic patterns of the domain-peptide interaction. To further illustrate the power and accuracy of our model, we used it to effectively engineer an exceptionally strong H3K9me3-binding chromodomain and to label H3K9me3 in live cells. This study presents a systematic approach to deciphering domain-peptide recognition and reveals a general principle by which histone modifications are interpreted by reader proteins, leading to dynamic regulation of gene expression and other biological processes.

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Vlachonasios, Konstantinos, Stylianos Poulios, and Niki Mougiou. "The Histone Acetyltransferase GCN5 and the Associated Coactivators ADA2: From Evolution of the SAGA Complex to the Biological Roles in Plants." Plants 10, no. 2 (February 5, 2021): 308. http://dx.doi.org/10.3390/plants10020308.

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Transcription of protein-encoding genes starts with forming a pre-initiation complex comprised of RNA polymerase II and several general transcription factors. To activate gene expression, transcription factors must overcome repressive chromatin structure, which is accomplished with multiprotein complexes. One such complex, SAGA, modifies the nucleosomal histones through acetylation and other histone modifications. A prototypical histone acetyltransferase (HAT) known as general control non-repressed protein 5 (GCN5), was defined biochemically as the first transcription-linked HAT with specificity for histone H3 lysine 14. In this review, we analyze the components of the putative plant SAGA complex during plant evolution, and current knowledge on the biological role of the key components of the HAT module, GCN5 and ADA2b in plants, will be summarized.

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Tanaka, M., J. D. Hennebold, J. Macfarlane, and E. Y. Adashi. "A mammalian oocyte-specific linker histone gene H1oo: homology with the genes for the oocyte-specific cleavage stage histone (cs-H1) of sea urchin and the B4/H1M histone of the frog." Development 128, no. 5 (March 1, 2001): 655–64. http://dx.doi.org/10.1242/dev.128.5.655.

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Oocytes and early embryos of multiple (non-mammalian) species lack the somatic form of the linker histone H1. To the best of our knowledge, a mammalian oocyte-specific linker (H1) histone(s) has not, as yet, been reported. We have uncovered the cDNA in question in the course of a differential screening (suppression subtractive hybridization (SSH)) project. Elucidation of the full-length sequence of this novel 1.2 kb cDNA led to the identification of a 912 bp open reading frame. The latter encoded a novel 34 kDa linker histone protein comprised of 304 amino acids, tentatively named H1oo. Amino acid BLAST analysis revealed that H1oo displayed the highest sequence homology to the oocyte-specific B4 histone of the frog, the respective central globular (putative DNA binding) domains displaying 54% identity. Substantial homology to the cs-H1 protein of the sea urchin oocyte was also apparent. While most oocytic mRNAs corresponding to somatic linker histones are not polyadenylated (and remain untranslated), the mRNAs of (non-mammalian) oocyte-specific linker histones and of mammalian H1oo, are polyadenylated, a process driven by the consensus signal sequence, AAUAAA, detected in the 3′-untranslated region of the H1oo cDNA. Our data suggest that the mouse oocyte-specific linker histone H1oo (1) constitutes a novel mammalian homolog of the oocyte-specific linker histone B4 of the frog and of the cs-H1 linker histone of the sea urchin; (2) is expressed as early as the GV (PI) stage oocyte, persisting into the MII stage oocyte, the oocytic polar bodies, and the two-cell embryo, extinction becoming apparent at the four- to eight-cell embryonic stage; and (3) may play a key role in the control of gene expression during oogenesis and early embryogenesis, presumably through the perturbation of chromatin structure.

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Rodríguez-Paredes, Manuel, and Frank Lyko. "The importance of non-histone protein methylation in cancer therapy." Nature Reviews Molecular Cell Biology 20, no. 10 (July 3, 2019): 569–70. http://dx.doi.org/10.1038/s41580-019-0147-x.

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Narita, Takeo, Brian T. Weinert, and Chunaram Choudhary. "Author Correction: Functions and mechanisms of non-histone protein acetylation." Nature Reviews Molecular Cell Biology 20, no. 8 (July 2, 2019): 508. http://dx.doi.org/10.1038/s41580-019-0156-9.

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Kiliańska, Zofia, Robert C. Briggs, and Lubomir S. Hnilica. "Specificity of non-histone protein antigens in chicken liver nuclei." International Journal of Biochemistry 19, no. 10 (January 1987): 995–99. http://dx.doi.org/10.1016/0020-711x(87)90183-2.

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Lee, Hyang Woo, Sung-Youl Hong, Sangduk Kim, and Woon Ki Paik. "Studies on unknown methylated compounds of non-histone nuclear protein." Archives of Pharmacal Research 8, no. 3 (September 1985): 149–57. http://dx.doi.org/10.1007/bf02857040.

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Jiang, Xuanzhao, Tatiana A. Soboleva, and David J. Tremethick. "Short Histone H2A Variants: Small in Stature but not in Function." Cells 9, no. 4 (April 2, 2020): 867. http://dx.doi.org/10.3390/cells9040867.

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The dynamic packaging of DNA into chromatin regulates all aspects of genome function by altering the accessibility of DNA and by providing docking pads to proteins that copy, repair and express the genome. Different epigenetic-based mechanisms have been described that alter the way DNA is organised into chromatin, but one fundamental mechanism alters the biochemical composition of a nucleosome by substituting one or more of the core histones with their variant forms. Of the core histones, the largest number of histone variants belong to the H2A class. The most divergent class is the designated “short H2A variants” (H2A.B, H2A.L, H2A.P and H2A.Q), so termed because they lack a H2A C-terminal tail. These histone variants appeared late in evolution in eutherian mammals and are lineage-specific, being expressed in the testis (and, in the case of H2A.B, also in the brain). To date, most information about the function of these peculiar histone variants has come from studies on the H2A.B and H2A.L family in mice. In this review, we describe their unique protein characteristics, their impact on chromatin structure, and their known functions plus other possible, even non-chromatin, roles in an attempt to understand why these peculiar histone variants evolved in the first place.

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Meheus, L. A., J. J. Van Beeumen, A. V. Coomans, and J. R. Vanfleteren. "Age-specific nuclear proteins in the nematode worm Caenorhabditis elegans." Biochemical Journal 245, no. 1 (July 1, 1987): 257–61. http://dx.doi.org/10.1042/bj2450257.

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The nematode worm Caenorhabditis elegans is known to undergo characteristic morphological as well as physiological signs of senescence. Two-dimensional gel electrophoresis shows that alterations also occur in the pattern of the nuclear proteins as a function of age. Non-histone proteins whose level exhibits a steep fall with age are egg-specific and not involved in senescence. However, a distinct set of non-histones accumulates with age and can be considered as senescence markers. Some of these are glycoproteins, as shown by their concanavalin A-binding properties. One age-specific polypeptide, called ‘protein S-28’, was further characterized by peptide mapping and determination of its N-terminal amino acid sequence.

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Jethmalani, Yogita, and Erin M. Green. "Using Yeast to Define the Regulatory Role of Protein Lysine Methylation." Current Protein & Peptide Science 21, no. 7 (September 23, 2020): 690–98. http://dx.doi.org/10.2174/1389203720666191023150727.

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The post-translational modifications (PTM) of proteins are crucial for cells to survive under diverse environmental conditions and to respond to stimuli. PTMs are known to govern a broad array of cellular processes including signal transduction and chromatin regulation. The PTM lysine methylation has been extensively studied within the context of chromatin and the epigenetic regulation of the genome. However, it has also emerged as a critical regulator of non-histone proteins important for signal transduction pathways. While the number of known non-histone protein methylation events is increasing, the molecular functions of many of these modifications are not yet known. Proteomic studies of the model system Saccharomyces cerevisiae suggest lysine methylation may regulate a diversity of pathways including transcription, RNA processing, translation, and signal transduction cascades. However, there has still been relatively little investigation of lysine methylation as a broad cellular regulator beyond chromatin and transcription. Here, we outline our current state of understanding of non-histone protein methylation in yeast and propose ways in which the yeast system can be leveraged to develop a much more complete picture of molecular mechanisms through which lysine methylation regulates cellular functions.

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Vasileva, Bela, Dessislava Staneva, Natalia Krasteva, George Miloshev, and Milena Georgieva. "Changes in Chromatin Organization Eradicate Cellular Stress Resilience to UVA/B Light and Induce Premature Aging." Cells 10, no. 7 (July 11, 2021): 1755. http://dx.doi.org/10.3390/cells10071755.

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Complex interactions among DNA and nuclear proteins maintain genome organization and stability. The nuclear proteins, particularly the histones, organize, compact, and preserve the stability of DNA, but also allow its dynamic reorganization whenever the nuclear processes require access to it. Five histone classes exist and they are evolutionarily conserved among eukaryotes. The linker histones are the fifth class and over time, their role in chromatin has been neglected. Linker histones interact with DNA and the other histones and thus sustain genome stability and nuclear organization. Saccharomyces cerevisiae is a brilliant model for studying linker histones as the gene for it is a single-copy and is non-essential. We, therefore, created a linker histone-free yeast strain using a knockout of the relevant gene and traced the way cells age chronologically. Here we present our results demonstrating that the altered chromatin dynamics during the chronological lifespan of the yeast cells with a mutation in ARP4 (the actin-related protein 4) and without the gene HHO1 for the linker histone leads to strong alterations in the gene expression profiles of a subset of genes involved in DNA repair and autophagy. The obtained results further prove that the yeast mutants have reduced survival upon UVA/B irradiation possibly due to the accelerated decompaction of chromatin and impaired proliferation. Our hypothesis posits that the higher-order chromatin structure and the interactions among chromatin proteins are crucial for the maintenance of chromatin organization during chronological aging under optimal and UVA-B stress conditions.

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Wallberg, A. E., E. M. Flinn, J. Å. Gustafsson, and A. P. H. Wright. "Recruitment of chromatin remodelling factors during gene activation via the glucocorticoid receptor N-terminal domain." Biochemical Society Transactions 28, no. 4 (August 1, 2000): 410–14. http://dx.doi.org/10.1042/bst0280410.

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We have shown that yeast mutants with defects in the Ada adaptor proteins are defective in hormone-dependent gene activation by ectopically expressed human glucocorticoid receptor (GR). Others have shown that the Ada2 protein is required for physical interactions between some activation domains and TBP (TATA-binding protein), whereas the Gcn5 (Ada4) protein has a histone acetyltransferase (HAT) activity. Although all HAT enzymes are able to acetylate histone substrates, some also acetylate non-histone proteins. Taken together, these observations suggest that the Ada proteins have the ability to effect different steps in the process of gene activation. It has recently been shown that the Ada proteins are present in two distinct protein complexes, the Ada complex and a larger SAGA complex. Our recent work has focused on determining (1) which of the Ada-containing complexes mediates gene activation by GR, (2) whether the HAT activity encoded by GCN5 is required for GR-dependent gene activation, (3) whether the Ada proteins contribute to GR-mediated activation at the level of chromatin remodelling and (4) how the role of these HAT complexes is integrated with other chromatin remodelling activities during GR-mediated gene activation. Our results suggest a model in which GR recruits the SAGA complex and that this contributes to chromatin remodelling via a mechanism involving the acetylation of histones. Furthermore, recruitment of the SWI/SNF remodelling complex also has a role in GR-mediated activation that is independent of the role of SAGA. These complexes are similar to analogous mammalian complexes and therefore these results are likely to be relevant to the human system.

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Pastorelli, Roberta, Germano Ferrari, Antonella Gozzini, Donatella Tombaccini, Valeria Santini, and Alberto Bosi. "CML Blasts Modify the Acetylation Pattern of Non Histone Proteins after Short Chain Fatty Acid Histone Deacetylase Inhibitor Treatment." Blood 106, no. 11 (November 16, 2005): 2884. http://dx.doi.org/10.1182/blood.v106.11.2884.2884.

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Abstract Imatinib is an effective therapy for chronic phase CML, but patients may became irresponsive due to the development of resistance, caused by amplification of the BCR-ABL genomic locus or by point mutations within the kinase domain of BCR-ABL, which prevents drug binding. Novel dual SRC/ABL kinase inhibitors with higher potency against native and imatinib-resistant mutants of BCR-ABL have substantial clinical utility, but at least one mutation remains resistant to any kinase inhibitor (T315I). Thus, the search for alternative drugs effective in CML is still cogent. Treatment of CML cells with histone deacetylase inhibitors (HDIs) of the class of hydroxamic acid analogues promotes proteasomal degradation of Bcr-Abl, associated with apoptosis, in synergy with imatinib. We evaluated whether HDIs of other classes, namely short chain fatty acids like butyrates and valproic acid, could exert the same effects and we intended to dissect the determining molecular mechanisms. The human CML cell lines K562, KBM, LAMA-84 S and LAMA-84 R and primary imatinib-resistant CML-BC cells were grown in the presence of valproic acid (VPA) at the escalating doses 0.2 mM to 2mM or the mannose ester of butyric acid D1 (0.2–1mM) for 24 and 48 hrs. Apoptosis was induced in a time and dose dependent manner by VPA and D1 (annexin V test and flow cytometric analysis after propidium iodide uptake). Imatinib was synergistic with both HDIs in inducing apoptosis and cell proliferation arrest (MTT-assay). VPA and D1 were able to induce after 48 hrs of incubation a significant decrease in the number of copies of BCR-ABL determined by real time-PCR, paralleled by a substantial decrease in Bcr-Abl protein expression, shown in western blots of total cell lysates from CML cells. This decrease in the expression of protein kinase could account for the synergy with imatinib, but also for the reversal of resistance in mutated Bcr-Abl CML cells and is consistent with what previously observed. We also analysed the expression of Hsp-90 (protein chaperone of Bcr-Abl) and found it quantitatively unmodified but hyperacetylated by the treatment with both HDIs. As little is known of the ability of short chain fatty acids to induce acetylation of non-histone proteins, we compared the acetylated proteome of CML cells treated and not treated with HDIs, alone and in combination with imatinib, by 2D western blot versus a pan-acetylated antibody, followed by MALDI-TOF mass spectrometry for protein identification. 22 proteins were positively identified with a high degree of confidence, with the majority of these being cytoplasmic. At least two chaperone proteins were identified as target of acetylation after VPA and D1 treatment of CML cells, other targets were proteins involved in the synthesis and stability of RNA. Phosphorylation of proteins, evaluated by 2D western blot, was not significantly affected by HDIs. Short chain fatty acids are indeed not the most potent HDIs, but have been used successfully in clinical trials. Our observations contribute to the dissection of proteome modifications by HDIs and may help extrapolate the molecular effects of different HDIs on CML cells so to improve their use as single drugs or in combination with imatinib or new SRC/ABL inhibitors.

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Espel, Enric, Jordi Bernués, Josep A. Pérez-Pons, and Enrique Querol. "Binding of HMG14 non-histone protein to histones H2A, H2B, H1 and DNA in reconstituted chromatin." Biochemical and Biophysical Research Communications 132, no. 3 (November 1985): 1031–37. http://dx.doi.org/10.1016/0006-291x(85)91910-2.

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Chioccarelli, Teresa, Riccardo Pierantoni, Francesco Manfrevola, Veronica Porreca, Silvia Fasano, Rosanna Chianese, and Gilda Cobellis. "Histone Post-Translational Modifications and CircRNAs in Mouse and Human Spermatozoa: Potential Epigenetic Marks to Assess Human Sperm Quality." Journal of Clinical Medicine 9, no. 3 (February 27, 2020): 640. http://dx.doi.org/10.3390/jcm9030640.

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Spermatozoa (SPZ) are motile cells, characterized by a cargo of epigenetic information including histone post-translational modifications (histone PTMs) and non-coding RNAs. Specific histone PTMs are present in developing germ cells, with a key role in spermatogenic events such as self-renewal and commitment of spermatogonia (SPG), meiotic recombination, nuclear condensation in spermatids (SPT). Nuclear condensation is related to chromatin remodeling events and requires a massive histone-to-protamine exchange. After this event a small percentage of chromatin is condensed by histones and SPZ contain nucleoprotamines and a small fraction of nucleohistone chromatin carrying a landascape of histone PTMs. Circular RNAs (circRNAs), a new class of non-coding RNAs, characterized by a nonlinear back-spliced junction, able to play as microRNA (miRNA) sponges, protein scaffolds and translation templates, have been recently characterized in both human and mouse SPZ. Since their abundance in eukaryote tissues, it is challenging to deepen their biological function, especially in the field of reproduction. Here we review the critical role of histone PTMs in male germ cells and the profile of circRNAs in mouse and human SPZ. Furthermore, we discuss their suggested role as novel epigenetic biomarkers to assess sperm quality and improve artificial insemination procedure.

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OHYAMA, Tamami, and Keiko SAKUMA. "Effects of a low-protein diet on chromosomal non-histone proteins in rat liver." Nippon Eiyo Shokuryo Gakkaishi 42, no. 1 (1989): 33–38. http://dx.doi.org/10.4327/jsnfs.42.33.

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Dong, Wenbo, Punit Prasad, Andreas Lennartsson, and Karl Ekwall. "The Role of Non-Catalytic Domains of Hrp3 in Nucleosome Remodeling." International Journal of Molecular Sciences 22, no. 4 (February 11, 2021): 1793. http://dx.doi.org/10.3390/ijms22041793.

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The Helicase-related protein 3 (Hrp3), an ATP-dependent chromatin remodeling enzyme from the CHD family, is crucial for maintaining global nucleosome occupancy in Schizosaccharomyces pombe (S. pombe). Although the ATPase domain of Hrp3 is essential for chromatin remodeling, the contribution of non-ATPase domains of Hrp3 is still unclear. Here, we investigated the role of non-ATPase domains using in vitro methods. In our study, we expressed and purified recombinant S. pombe histone proteins, reconstituted them into histone octamers, and assembled nucleosome core particles. Using reconstituted nucleosomes and affinity-purified wild type and mutant Hrp3 from S. pombe we created a homogeneous in vitro system to evaluate the ATP hydrolyzing capacity of truncated Hrp3 proteins. We found that all non-ATPase domain deletions (∆chromo, ∆SANT, ∆SLIDE, and ∆coupling region) lead to reduced ATP hydrolyzing activities in vitro with DNA or nucleosome substrates. Only the coupling region deletion showed moderate stimulation of ATPase activity with the nucleosome. Interestingly, affinity-purified Hrp3 showed co-purification with all core histones suggesting a strong association with the nucleosomes in vivo. However, affinity-purified Hrp3 mutant with SANT and coupling regions deletion showed complete loss of interactions with the nucleosomes, while SLIDE and chromodomain deletions reduced Hrp3 interactions with the nucleosomes. Taken together, nucleosome association and ATPase stimulation by DNA or nucleosomes substrate suggest that the enzymatic activity of Hrp3 is fine-tuned by unique contributions of all four non-catalytic domains.

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Song, Wan, Nóra Zsindely, Anikó Faragó, J. Lawrence Marsh, and László Bodai. "Systematic genetic interaction studies identify histone demethylase Utx as potential target for ameliorating Huntington’s disease." Human Molecular Genetics 27, no. 4 (December 21, 2017): 649–66. http://dx.doi.org/10.1093/hmg/ddx432.

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Abstract Huntington’s disease (HD) is a dominantly inherited neurodegenerative disease caused by alterations in the huntingtin gene (htt). Transcriptional dysregulation is an early event in HD progression. Protein acetylation and methylation particularly on histones regulates chromatin structure thereby preventing or facilitating transcription. Although protein acetylation has been found to affect HD symptoms, little is known about the potential role of protein methylation in HD pathology. In recent years, a series of proteins have been described that are responsible for methylating and demethylating histones as well as other proteins. We carried out systematic genetic interaction studies testing lysine and arginine methylases and demethylases in a Drosophila melanogaster HD model. We found that modulating methylation enzymes that typically affect histone positions H3K4, H3K36 or H3K79 had varying effects on HD pathology while modulating ones that typically affect constitutive heterochromatin marks at H3K9 and H4K20 generally had limited impact on HD pathology. In contrast, modulating enzymes acting on the facultative heterochromatin mark at H3K27 had specific effects on HD pathology, with reduction of the demethylase Utx rescuing HTT-induced pathology while reducing Polycomb Repressive Complex2 core methylase components led to more aggressive pathology. Further exploration of the mechanism underlying the methylation-specific interactions suggest that these lysine and arginine methylases and demethylases are likely exerting their influence through non-histone targets. These results highlight a novel therapeutic approach for HD in the form of Utx inhibition.

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Hamamoto, Ryuji, Vassiliki Saloura, and Yusuke Nakamura. "Critical roles of non-histone protein lysine methylation in human tumorigenesis." Nature Reviews Cancer 15, no. 2 (January 23, 2015): 110–24. http://dx.doi.org/10.1038/nrc3884.

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Iancu-Rubin, Camelia, Faye Feller, David Gajzer, John Mascarenhas, and Ronald Hoffman. "Targeting Non-Histone Protein Acetylation Impairs Platelet Production During Normal Megakaryocytopoiesis." Blood 116, no. 21 (November 19, 2010): 2610. http://dx.doi.org/10.1182/blood.v116.21.2610.2610.

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Abstract Abstract 2610 Megakaryocytopoiesis consists of a succession of events in which MK progenitors initially proliferate and acquire lineage-specific markers, followed by polyploidization and cytoplasmic maturation. MK maturation culminates in the formation of cytoplasmic extensions (i.e. proplatelets) that leads to platelet shedding into the circulation. Panobinostat (LBH589) is a histone deacetylase inhibitor that has antiproliferative and cytotoxic effects on several types of cancer cells including blood cells from patients with hematological malignancies. One of the major adverse events associated with LBH589 treatment is thrombocytopenia. In this study, we hypothesize that the effects of LBH589 on thrombopoiesis might occur by targeting acetylation of histone and/or non-histone proteins resulting in defective platelet production. To test this hypothesis we investigated the effects of LBH589 on megakaryocytopoiesis in MK cell lines (i.e. HEL JAK2V617F positive cells) and in primary human MK. First, we tested the effects of LBH589 on the ability of human CD34+ cells to generate MK colony forming units (CFU-MKs). Neither CFU-MK or CFU-MIX derived colony formation was reduced in the presence of LBH589. To evaluate the effects of LBH589 on parameters of MK maturation, MK were generated in vitro from peripheral blood-derived CD34+ cells by employing an expansion culture system containing SCF and TPO for 6 days followed by 8 additional days incubation in the presence of TPO. These studies were pursued in the presence or absence of LBH589. Treatment with LBH589 did not significantly influence the number of CD61+ MK (i.e. control = 55.8%; 2.5nM LBH589 = 45.2%, p value=0.109; 5nM LBH589=38.5%, p value=0.095, of viable 7-AAD−/CD61+ cells) or the degree of polyploidization (i.e. control = 17.4%; 2.5nM LBH589 = 14.4%86.7, p value=0.157; 5nM LBH 589=12.8%, p value=0.116, cells with >4N DNA content). Culture-derived platelets were analyzed phenotypically and quantitated by means of dual labeling with anti-CD41 antibodies and with thiazole orange (TO) in order to identify new reticulated platelets. The percentage of CD41+/TO+ platelets derived from MK generated in the presence of LBH589 was significantly reduced (i.e. 2.5nM LBH589=11%, p value 0.046 and 5nM LBH589=9%, p value=0.011, CD41+/TO+ cells) as compared with MK generated in the absence of LBH589 (18.5% CD41+/TO+ cells). These findings were consistent with the observation of significant numbers of proplatelet-bearing MKs in control cultures but not in LBH 589-treated cultures. Collectively, these data suggest that LBH589 impairs platelet production while having a minimal effect on MK commitment, cytoplasmic maturation or polyploidization. To better understand the mechanisms responsible for such effects on thrombopoiesis, RNA extracted from control MK and from MK treated in vitro with LBH589 was analyzed by real time quantitative PCR to evaluate GATA-1 and NF-E2 expression. GATA-1 and NF-E2 mRNA levels were unchanged after treatment with LBH589. We found, however, that LBH589 induced a 4.8 to 7.5-fold increase in histone H3 acetylation. These data suggest that the negative impact of LBH589 on MK maturation was not mediated by its effects on chromatin but rather was possibly due to its effects on acetylation of nonhistone proteins. We demonstrated that LBH589 treatment increased acetylation of tubulin, a non-histone cytoplasmic protein that is a component of the microtubule (MT) cytoskeleton. The later stages of MK maturation are highly dependent on MT which represent the structural scaffold for proplatelet extension and enables the transport of cytoplasmic organelles into nascent platelets. The changes in the acetylation status of tubulin are critical for proper MT function and are mediated by HDAC6 which we found by Western blot analysis to be inhibited by LBH589 treatment. Based on these findings we suggest that LBH589-induced changes in tubulin acetylation result in aberrant MT function which in turn, leads to defective proplatelet and platelet formation. These nonhistone protein modifications might serve as a drug target for the development of novel agents (LBH589) to treat patients with extreme thrombocytosis due to underlying myeloproliferative neoplasms. Disclosures: Iancu-Rubin: Novartis: Research Funding. Hoffman:Novartis: Research Funding.

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Pogorelova, T. N., V. O. Gunko, A. A. Nikashina, A. A. Mikhelson, I. A. Alliluev, and A. V. Larichkin. "Impairment of production and posttranslational changes of placental nuclear and membrane proteins with complicated pregnancy." Biomeditsinskaya Khimiya 65, no. 6 (2019): 513–19. http://dx.doi.org/10.18097/pbmc20196506513.

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The content of nuclear and membrane proteins of the placenta, as well as posttranslational modification of these proteins in physiological pregnancy and placental insufficiency (PI) were studied. Differential centrifugation, electrophoresis in polyacrylamide gel, spectrophotometric methods were used. It was found that with PN there is a decrease in the degree of production of the studied proteins of varying degrees relative to control parameters. For chromatin proteins, a more pronounced decrease in the content of non-histone proteins was found in comparison with histones. Among histone fractions, the maximum decrease was detected in the H2A fraction. The degree of change in the amount of membrane proteins depends on the detergent used. Changes in posttranslational protein modifications disorders are characterized by a decrease in the content of amine and amide (especially difficult to hydrolyze) groups and an increase in carbonyl derivatives of proteins. The revealed changes in the composition and structure of the nuclear and membrane proteins of the placenta, performing numerous regulatory functions, can be triggering links in the chain of molecular damage in the placenta at PI.

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Journal articles on the topic 'Non histone protein'

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