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Journal articles on the topic 'Histone post-translational modifications (hPTMs)'

Author: Grafiati

Published: 9 March 2023

Last updated: 31 July 2025

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1

Hu, Qiwen, Casey S. Greene, and Elizabeth A. Heller. "Specific histone modifications associate with alternative exon selection during mammalian development." Nucleic Acids Research 48, no. 9 (2020): 4709–24. http://dx.doi.org/10.1093/nar/gkaa248.

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Abstract Alternative splicing (AS) is frequent during early mouse embryonic development. Specific histone post-translational modifications (hPTMs) have been shown to regulate exon splicing by either directly recruiting splice machinery or indirectly modulating transcriptional elongation. In this study, we hypothesized that hPTMs regulate expression of alternatively spliced genes for specific processes during differentiation. To address this notion, we applied an innovative machine learning approach to relate global hPTM enrichment to AS regulation during mammalian tissue development. We found

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Andonegui-Elguera, Marco A., Rodrigo E. Cáceres-Gutiérrez, Alejandro López-Saavedra, et al. "The Roles of Histone Post-Translational Modifications in the Formation and Function of a Mitotic Chromosome." International Journal of Molecular Sciences 23, no. 15 (2022): 8704. http://dx.doi.org/10.3390/ijms23158704.

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During mitosis, many cellular structures are organized to segregate the replicated genome to the daughter cells. Chromatin is condensed to shape a mitotic chromosome. A multiprotein complex known as kinetochore is organized on a specific region of each chromosome, the centromere, which is defined by the presence of a histone H3 variant called CENP-A. The cytoskeleton is re-arranged to give rise to the mitotic spindle that binds to kinetochores and leads to the movement of chromosomes. How chromatin regulates different activities during mitosis is not well known. The role of histone post-transl

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Ghiani, Lavinia, and Susanna Chiocca. "High Risk-Human Papillomavirus in HNSCC: Present and Future Challenges for Epigenetic Therapies." International Journal of Molecular Sciences 23, no. 7 (2022): 3483. http://dx.doi.org/10.3390/ijms23073483.

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Head and Neck Squamous Cell Carcinoma (HNSCC) is a highly heterogeneous group of tumors characterized by an incidence of 650,000 new cases and 350,000 deaths per year worldwide and a male to female ratio of 3:1. The main risk factors are alcohol and tobacco consumption and Human Papillomavirus (HPV) infections. HNSCC cases are divided into two subgroups, the HPV-negative (HPV−) and the HPV-positive (HPV+) which have different clinicopathological and molecular profiles. However, patients are still treated with the same therapeutic regimens. It is thus of utmost importance to characterize the mo

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Tibana, Ramires, Octávio Franco, Rinaldo Pereira, James Navalta, and Jonato Prestes. "Exercise as an Effective Transgenerational Strategy to Overcome Metabolic Syndrome in the Future Generation: Are We There?" Experimental and Clinical Endocrinology & Diabetes 125, no. 06 (2017): 347–52. http://dx.doi.org/10.1055/s-0042-120538.

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AbstractMetabolic syndrome (MetS) consist in a combination of cardiovascular risk factors including elevated blood pressure, dyslipidemia, insulin resistance, hyperglycemia and abdominal obesity. Exercise performed before, during and after pregnancy can exert positive effects to counteract MetS risk factors. Here this review aims to analyze the effects of exercise performed before (fathers and mothers) and after periconception (mothers) by using experimental models and its effects on MetS risk factors in offspring. All selected studies investigated the effects of aerobic exercise before, durin

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Agnusdei, Angelo, Adrián González-García, Donato Gerin, et al. "Histone Methyltransferases AcDot1 and AcRmtA Are Involved in Growth Regulation, Secondary Metabolism, and Stress Response in Aspergillus carbonarius." Toxins 17, no. 4 (2025): 196. https://doi.org/10.3390/toxins17040196.

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Histone post-translational modifications (HPTMs) can affect gene expression by rearranging chromatin structure. Between these, histone methylation is one of the most studied in filamentous fungi, and different conserved domains coding for methyltransferase were found in Aspergillus spp. genomes. In this work, the role of the histone methyltransferases AcDot1 and AcRmtA in the mycotoxigenic fungus Aspergillus carbonarius was investigated, obtaining knockout or overexpression mutants through Agrobacterium tumefaciens-mediated transformation (ATMT). A. carbonarius is responsible for grape-bunch r

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Gaona-López, Carlos, Lenci K. Vazquez-Jimenez, Alonzo Gonzalez-Gonzalez, et al. "Advances in Protozoan Epigenetic Targets and Their Inhibitors for the Development of New Potential Drugs." Pharmaceuticals 16, no. 4 (2023): 543. http://dx.doi.org/10.3390/ph16040543.

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Protozoan parasite diseases cause significant mortality and morbidity worldwide. Factors such as climate change, extreme poverty, migration, and a lack of life opportunities lead to the propagation of diseases classified as tropical or non-endemic. Although there are several drugs to combat parasitic diseases, strains resistant to routinely used drugs have been reported. In addition, many first-line drugs have adverse effects ranging from mild to severe, including potential carcinogenic effects. Therefore, new lead compounds are needed to combat these parasites. Although little has been studie

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Taylor, Bethany C., and Nicolas L. Young. "Combinations of histone post-translational modifications." Biochemical Journal 478, no. 3 (2021): 511–32. http://dx.doi.org/10.1042/bcj20200170.

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Histones are essential proteins that package the eukaryotic genome into its physiological state of nucleosomes, chromatin, and chromosomes. Post-translational modifications (PTMs) of histones are crucial to both the dynamic and persistent regulation of the genome. Histone PTMs store and convey complex signals about the state of the genome. This is often achieved by multiple variable PTM sites, occupied or unoccupied, on the same histone molecule or nucleosome functioning in concert. These mechanisms are supported by the structures of ‘readers’ that transduce the signal from the presence or abs

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Hattori, Takamitsu, Joseph M. Taft, Kalina M. Swist, et al. "Recombinant antibodies to histone post-translational modifications." Nature Methods 10, no. 10 (2013): 992–95. http://dx.doi.org/10.1038/nmeth.2605.

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Fan, Jing, Kimberly A. Krautkramer, Jessica L. Feldman, and John M. Denu. "Metabolic Regulation of Histone Post-Translational Modifications." ACS Chemical Biology 10, no. 1 (2015): 95–108. http://dx.doi.org/10.1021/cb500846u.

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Abaturov, O. E., and A. O. Nikulina. "Post-translational histone modifications associated with the development of metabolic dysfunction-associated fatty liver disease. Part 1. General provisions." GASTROENTEROLOGY 58, no. 3 (2024): 210–21. http://dx.doi.org/10.22141/2308-2097.58.3.2024.626.

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Based on the analysis of literary sources of PubMed, MedLine, The Cochrane Library, EMBASE database, the authors of the article give general provisions regarding post-translational modifications of histones (small proteins with a molecular weight of 10–15 kDa, which make up the largest part of nuclear proteins), which are associated with the development of metabolic dysfunction-associated fatty liver disease. The authors emphasize that post-translational histone modifications regulate the activity of gene expression, and each of these types differently changes the structure of chromatin and, a

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Tolsma, Thomas O., and Jeffrey C. Hansen. "Post-translational modifications and chromatin dynamics." Essays in Biochemistry 63, no. 1 (2019): 89–96. http://dx.doi.org/10.1042/ebc20180067.

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Abstract The dynamic structure of chromatin is linked to gene regulation and many other biological functions. Consequently, it is of importance to understand the factors that regulate chromatin dynamics. While the in vivo analysis of chromatin has verified that histone post-translational modifications play a role in modulating DNA accessibility, the complex nuclear environment and multiplicity of modifications prevents clear conclusions as to how individual modifications influence chromatin dynamics in the cell. For this reason, in vitro analyses of model reconstituted nucleosomal arrays has b

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Liu, Yanli, and Jinrong Min. "Structure and function of histone methylation-binding proteins in plants." Biochemical Journal 473, no. 12 (2016): 1663–80. http://dx.doi.org/10.1042/bcj20160123.

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Post-translational modifications of histones play important roles in modulating many essential biological processes in both animals and plants. These covalent modifications, including methylation, acetylation, phosphorylation, ubiquitination, SUMOylation and so on, are laid out and erased by histone-modifying enzymes and read out by effector proteins. Recent studies have revealed that a number of developmental processes in plants are under the control of histone post-translational modifications, such as floral transition, seed germination, organogenesis and morphogenesis. Therefore, it is crit

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Zhiteneva, Alisa, Juan Jose Bonfiglio, Alexandr Makarov, et al. "Mitotic post-translational modifications of histones promote chromatin compaction in vitro." Open Biology 7, no. 9 (2017): 170076. http://dx.doi.org/10.1098/rsob.170076.

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How eukaryotic chromosomes are compacted during mitosis has been a leading question in cell biology since the nineteenth century. Non-histone proteins such as condensin complexes contribute to chromosome shaping, but appear not to be necessary for mitotic chromatin compaction. Histone modifications are known to affect chromatin structure. As histones undergo major changes in their post-translational modifications during mitotic entry, we speculated that the spectrum of cell-cycle-specific histone modifications might contribute to chromosome compaction during mitosis. To test this hypothesis, w

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Andrés, Marta, Daniel García-Gomis, Inma Ponte, Pedro Suau, and Alicia Roque. "Histone H1 Post-Translational Modifications: Update and Future Perspectives." International Journal of Molecular Sciences 21, no. 16 (2020): 5941. http://dx.doi.org/10.3390/ijms21165941.

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Histone H1 is the most variable histone and its role at the epigenetic level is less characterized than that of core histones. In vertebrates, H1 is a multigene family, which can encode up to 11 subtypes. The H1 subtype composition is different among cell types during the cell cycle and differentiation. Mass spectrometry-based proteomics has added a new layer of complexity with the identification of a large number of post-translational modifications (PTMs) in H1. In this review, we summarize histone H1 PTMs from lower eukaryotes to humans, with a particular focus on mammalian PTMs. Special emp

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Hamam and Palaniyar. "Post-Translational Modifications in NETosis and NETs-Mediated Diseases." Biomolecules 9, no. 8 (2019): 369. http://dx.doi.org/10.3390/biom9080369.

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: Neutrophils undergo a unique form of cell death that generates neutrophil extracellular traps (NETs) that may help to neutralize invading pathogens and restore homeostasis. However, uncontrolled NET formation (NETosis) can result in numerous diseases that adversely affect health. Recent studies further elucidate the mechanistic details of the different forms of NETosis and their common end structure, as NETs were constantly found to contain DNA, modified histones and cytotoxic enzymes. In fact, emerging evidence reveal that the post translational modifications (PTMs) of histones in neutrophi

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Méndez-Acuña, L., M. V. Di Tomaso, F. Palitti, and W. Martínez-López. "Histone Post-Translational Modifications in DNA Damage Response." Cytogenetic and Genome Research 128, no. 1-3 (2010): 28–36. http://dx.doi.org/10.1159/000296275.

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da Cunha, Julia Pinheiro Chagas, Ernesto Satoshi Nakayasu, Igor Correia de Almeida, and Sergio Schenkman. "Post-translational modifications of Trypanosoma cruzi histone H4." Molecular and Biochemical Parasitology 150, no. 2 (2006): 268–77. http://dx.doi.org/10.1016/j.molbiopara.2006.08.012.

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Sevilla, Ana, and Olivier Binda. "Post-translational modifications of the histone variant h2az." Stem Cell Research 12, no. 1 (2014): 289–95. http://dx.doi.org/10.1016/j.scr.2013.11.004.

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Minshull, Thomas C., and Mark J. Dickman. "Mass spectrometry analysis of histone post translational modifications." Drug Discovery Today: Disease Models 12 (2014): 41–48. http://dx.doi.org/10.1016/j.ddmod.2015.03.002.

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Bronner, Christian, Guy Fuhrmann, Frédéric L. Chédin, Marcella Macaluso, and Sirano Dhe-Paganon. "UHRF1 Links the Histone Code and DNA Methylation to Ensure Faithful Epigenetic Memory Inheritance." Genetics & Epigenetics 2 (January 2009): GEG.S3992. http://dx.doi.org/10.4137/geg.s3992.

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Epigenetics is the study of the transmission of cell memory through mitosis or meiosis that is not based on the DNA sequence. At the molecular level the epigenetic memory of a cell is embedded in DNA methylation, histone post-translational modifications, RNA interference and histone isoform variation. There is a tight link between histone post-translational modifications (the histone code) and DNA methylation, as modifications of histones contribute to the establishment of DNA methylation patterns and vice versa. Interestingly, proteins have recently been identified that can simultaneously rea

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Chatterjee, Snehajyoti, Parijat Senapati, and Tapas K. Kundu. "Post-translational modifications of lysine in DNA-damage repair." Essays in Biochemistry 52 (May 25, 2012): 93–111. http://dx.doi.org/10.1042/bse0520093.

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DNA damage in cells is often the result of constant genotoxic insult. Nevertheless, efficient DNA repair pathways are able to maintain genomic integrity. Over the past decade it has been revealed that it is not only kinase signalling pathways which play a central role in this process, but also the different post-translational modifications at lysine residues of histone (chromatin) and non-histone proteins. These lysine modifications include acetylation, methylation, ubiquitination and SUMOylation. Genomic instability is often the major cause of different diseases, especially cancer, where lysi

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Wang, Xiaodong, and Jeffrey J. Hayes. "Physical methods used to study core histone tail structures and interactions in solutionThis paper is one of a selection of papers published in this Special Issue, entitled 27th International West Coast Chromatin and Chromosome Conference, and has undergone the Journal's usual peer review process." Biochemistry and Cell Biology 84, no. 4 (2006): 578–88. http://dx.doi.org/10.1139/o06-076.

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The core histone tail domains are key regulatory elements in chromatin. The tails are essential for folding oligonucleosomal arrays into both secondary and tertiary structures, and post-translational modifications within these domains can directly alter DNA accessibility. Unfortunately, there is little understanding of the structures and interactions of the core histone tail domains or how post-translational modifications within the tails may alter these interactions. Here we review NMR, thermal denaturation, cross-linking, and other selected solution methods used to define the general structu

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Nothof, Sophie A., Frédérique Magdinier, and Julien Van-Gils. "Chromatin Structure and Dynamics: Focus on Neuronal Differentiation and Pathological Implication." Genes 13, no. 4 (2022): 639. http://dx.doi.org/10.3390/genes13040639.

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Chromatin structure is an essential regulator of gene expression. Its state of compaction contributes to the regulation of genetic programs, in particular during differentiation. Epigenetic processes, which include post-translational modifications of histones, DNA methylation and implication of non-coding RNA, are powerful regulators of gene expression. Neurogenesis and neuronal differentiation are spatio-temporally regulated events that allow the formation of the central nervous system components. Here, we review the chromatin structure and post-translational histone modifications associated

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García-Giménez, José-Luis, Concepción Garcés, Carlos Romá-Mateo, and Federico V. Pallardó. "Oxidative stress-mediated alterations in histone post-translational modifications." Free Radical Biology and Medicine 170 (July 2021): 6–18. http://dx.doi.org/10.1016/j.freeradbiomed.2021.02.027.

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Monti, Barbara. "Histone Post-translational Modifications to Target Memory-related Diseases." Current Pharmaceutical Design 19, no. 28 (2013): 5065–75. http://dx.doi.org/10.2174/1381612811319280005.

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Tian, Zhixin, Nikola Tolić, Rui Zhao, et al. "Enhanced top-down characterization of histone post-translational modifications." Genome Biology 13, no. 10 (2012): R86. http://dx.doi.org/10.1186/gb-2012-13-10-r86.

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Füllgrabe, Jens, Daniel J. Klionsky, and Bertrand Joseph. "Histone post-translational modifications regulate autophagy flux and outcome." Autophagy 9, no. 10 (2013): 1621–23. http://dx.doi.org/10.4161/auto.25803.

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Al-Kachak, Amni, and Ian Maze. "Post-translational modifications of histone proteins by monoamine neurotransmitters." Current Opinion in Chemical Biology 74 (June 2023): 102302. http://dx.doi.org/10.1016/j.cbpa.2023.102302.

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Draker, Ryan, and Peter Cheung. "Transcriptional and epigenetic functions of histone variant H2A.ZThis paper is one of a selection of papers published in this Special Issue, entitled CSBMCB’s 51st Annual Meeting – Epigenetics and Chromatin Dynamics, and has undergone the Journal’s usual peer review process." Biochemistry and Cell Biology 87, no. 1 (2009): 19–25. http://dx.doi.org/10.1139/o08-117.

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The chromatin organization of a genome ultimately dictates the gene expression profile of the cell. It is now well recognized that key mechanisms that regulate chromatin structure include post-translational modifications of histones and the incorporation of histone variants at strategic sites within the genome. H2A.Z is a variant of H2A that is localized to the 5′ end of many genes and is required for proper regulation of gene expression. However, its precise function in the transcription process is not yet well defined. In this review, we discuss some of the recent findings related to this hi

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Sales-Gil, Raquel, and Paola Vagnarelli. "How HP1 Post-Translational Modifications Regulate Heterochromatin Formation and Maintenance." Cells 9, no. 6 (2020): 1460. http://dx.doi.org/10.3390/cells9061460.

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Heterochromatin Protein 1 (HP1) is a highly conserved protein that has been used as a classic marker for heterochromatin. HP1 binds to di- and tri-methylated histone H3K9 and regulates heterochromatin formation, functions and structure. Besides the well-established phosphorylation of histone H3 Ser10 that has been shown to modulate HP1 binding to chromatin, several studies have recently highlighted the importance of HP1 post-translational modifications and additional epigenetic features for the modulation of HP1-chromatin binding ability and heterochromatin formation. In this review, we summar

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McManus, Kirk J., and Michael J. Hendzel. "The relationship between histone H3 phosphorylation and acetylation throughout the mammalian cell cycleThis paper is one of a selection of papers published in this Special Issue, entitled 27th International West Coast Chromatin and Chromosome Conference, and has undergone the Journal's usual peer review process." Biochemistry and Cell Biology 84, no. 4 (2006): 640–57. http://dx.doi.org/10.1139/o06-086.

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During interphase, histone amino-terminal tails play important roles in regulating the extent of DNA compaction. Post-translational modifications of the histone tails are intimately associated with regulating chromatin structure: phosphorylation of histone H3 is associated with proper chromosome condensation and dynamics during mitosis, while multiple H2B, H3, and H4 tail acetylations destabilize the chromatin fiber and are sufficient to decondense chromatin fibers in vitro. In this study, we investigate the spatio-temporal dynamics of specific histone H3 phosphorylations and acetylations to b

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Ito, K. "Impact of post-translational modifications of proteins on the inflammatory process." Biochemical Society Transactions 35, no. 2 (2007): 281–83. http://dx.doi.org/10.1042/bst0350281.

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PTM (post-translational modification) is the chemical modification of a protein after its translation. The well-studied PTM is phosphorylation, but, recently, PTMs have been re-focused by extensive studies on histone modifications and the discovery of the ubiquitin system. Histone acetylation is the well-established epigenetic regulator for gene expression. Recent studies show that different patterns of PTMs and cross-talk of individual modifications (acetylation, methylation, phosphorylation) are keys of gene regulation (known as the ‘histone code’). As well as histone, non-histone proteins a

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Bege, Miklós, and Anikó Borbás. "Medicines for influencing the posttranslational modifications of histones – a tutorial review." De Remediis 1, no. 1 (2024): 14. https://doi.org/10.71116/2rks7z60.

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Epigenetic therapy is a relatively novel, but undoubtedly a promising area of pharmacology. Most epigenetic drugs act by affecting enzymes and play a role in post-translational modifications of histones. The molecular targets of these medicines include histone methyltransferases, histone demethylases, isocitrate dehydrogenases, histone acetyltransferases and histone deacetylases. Since histone modifications are important regulatory signals, abnormalities in this process often lead to tumorigenesis, therefore these medicines constitute an important class of antitumor therapy. In this tutorial r

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Esteves de Lima, Joana, and Frédéric Relaix. "Epigenetic Regulation of Myogenesis: Focus on the Histone Variants." International Journal of Molecular Sciences 22, no. 23 (2021): 12727. http://dx.doi.org/10.3390/ijms222312727.

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Skeletal muscle development and regeneration rely on the successive activation of specific transcription factors that engage cellular fate, promote commitment, and drive differentiation. Emerging evidence demonstrates that epigenetic regulation of gene expression is crucial for the maintenance of the cell differentiation status upon division and, therefore, to preserve a specific cellular identity. This depends in part on the regulation of chromatin structure and its level of condensation. Chromatin architecture undergoes remodeling through changes in nucleosome composition, such as alteration

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Drury, Georgina E., Adam A. Dowle, David A. Ashford, Wanda M. Waterworth, Jerry Thomas, and Christopher E. West. "Dynamics of plant histone modifications in response to DNA damage." Biochemical Journal 445, no. 3 (2012): 393–401. http://dx.doi.org/10.1042/bj20111956.

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DNA damage detection and repair take place in the context of chromatin, and histone proteins play important roles in these events. Post-translational modifications of histone proteins are involved in repair and DNA damage signalling processes in response to genotoxic stresses. In particular, acetylation of histones H3 and H4 plays an important role in the mammalian and yeast DNA damage response and survival under genotoxic stress. However, the role of post-translational modifications to histones during the plant DNA damage response is currently poorly understood. Several different acetylated H

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Weaver, Tyler, Emma Morrison, and Catherine Musselman. "Reading More than Histones: The Prevalence of Nucleic Acid Binding among Reader Domains." Molecules 23, no. 10 (2018): 2614. http://dx.doi.org/10.3390/molecules23102614.

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The eukaryotic genome is packaged into the cell nucleus in the form of chromatin, a complex of genomic DNA and histone proteins. Chromatin structure regulation is critical for all DNA templated processes and involves, among many things, extensive post-translational modification of the histone proteins. These modifications can be “read out” by histone binding subdomains known as histone reader domains. A large number of reader domains have been identified and found to selectively recognize an array of histone post-translational modifications in order to target, retain, or regulate chromatin-mod

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Garcia, Benjamin A. "Mass Spectrometric Analysis of Histone Variants and Post-translational Modifications." Frontiers in Bioscience S1, no. 1 (2009): 142–53. http://dx.doi.org/10.2741/s14.

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Starkova, T. Yu, A. M. Polyanichko, T. O. Artamonova, et al. "Post-translational modifications of linker histone H1 variants in mammals." Physical Biology 14, no. 1 (2017): 016005. http://dx.doi.org/10.1088/1478-3975/aa551a.

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Fukagawa, Tatsuo. "Critical histone post-translational modifications for centromere function and propagation." Cell Cycle 16, no. 13 (2017): 1259–65. http://dx.doi.org/10.1080/15384101.2017.1325044.

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Chatterjee, A., N. Von Neuhoff, B. Skawran, L. Lauterboeck, N. Hofmann, and B. Glasmacher. "Cryopreservation alters the histone post-translational modifications of stem cells." Cryobiology 73, no. 3 (2016): 402. http://dx.doi.org/10.1016/j.cryobiol.2016.09.018.

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Perri, Angela Mena, Valter Agosti, Erika Olivo, et al. "Histone proteomics reveals novel post-translational modifications in breast cancer." Aging 11, no. 23 (2019): 11722–55. http://dx.doi.org/10.18632/aging.102577.

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Cobos, Samantha N., Seth A. Bennett, and Mariana P. Torrente. "The impact of histone post-translational modifications in neurodegenerative diseases." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1865, no. 8 (2019): 1982–91. http://dx.doi.org/10.1016/j.bbadis.2018.10.019.

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Galligan, James, James Wepy, Matthew Streeter, et al. "Methylglyoxal-derived post-translational arginine modifications are abundant histone marks." Free Radical Biology and Medicine 128 (November 2018): S137. http://dx.doi.org/10.1016/j.freeradbiomed.2018.10.362.

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Corujo, David, and Marcus Buschbeck. "Post-Translational Modifications of H2A Histone Variants and Their Role in Cancer." Cancers 10, no. 3 (2018): 59. http://dx.doi.org/10.3390/cancers10030059.

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Histone variants are chromatin components that replace replication-coupled histones in a fraction of nucleosomes and confer particular characteristics to chromatin. H2A variants represent the most numerous and diverse group among histone protein families. In the nucleosomal structure, H2A-H2B dimers can be removed and exchanged more easily than the stable H3-H4 core. The unstructured N-terminal histone tails of all histones, but also the C-terminal tails of H2A histones protrude out of the compact structure of the nucleosome core. These accessible tails are the preferential target sites for a

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Tersenidis, Christos, Stylianos Poulios, George Komis, Emmanuel Panteris, and Konstantinos Vlachonasios. "Roles of Histone Acetylation and Deacetylation in Root Development." Plants 13, no. 19 (2024): 2760. http://dx.doi.org/10.3390/plants13192760.

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Roots are usually underground plant organs, responsible for anchoring to the soil, absorbing water and nutrients, and interacting with the rhizosphere. During root development, roots respond to a variety of environmental signals, contributing to plant survival. Histone post-translational modifications play essential roles in gene expression regulation, contributing to plant responses to environmental cues. Histone acetylation is one of the most studied post-translational modifications, regulating numerous genes involved in various biological processes, including development and stress response

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Cobos, Samantha N., Chaim Janani, Gabriel Cruz, et al. "[PRION+] States Are Associated with Specific Histone H3 Post-Translational Modification Changes." Pathogens 11, no. 12 (2022): 1436. http://dx.doi.org/10.3390/pathogens11121436.

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Prions are proteins able to take on alternative conformations and propagate them in a self-templating process. In Saccharomyces cerevisiae, prions enable heritable responses to environmental conditions through bet-hedging mechanisms. Hence, [PRION+] states may serve as an atypical form of epigenetic control, producing heritable phenotypic change via protein folding. However, the connections between prion states and the epigenome remain unknown. Do [PRION+] states link to canonical epigenetic channels, such as histone post-translational modifications? Here, we map out the histone H3 modificatio

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Tirichine, L., X. Lin, Y. Thomas, B. Lombard, D. Loew, and C. Bowler. "Histone extraction protocol from the two model diatoms Phaeodactylum tricornutum and Thalassiosira pseudonana." Marine Genomics 13, no. 2014 (2014): 21–25. https://doi.org/10.1016/j.margen.2013.11.006.

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Post-translational modifications of histones affect many biological processes by influencing higher order chromatin structure that affects gene and genome regulation. It is therefore important to develop methods for extracting histones while maintaining their native post-translational modifications. While histone extraction protocols have been developed in multicellular and single celled organisms such as yeast and Arabidopsis, they are inefficient in diatoms that have a silica cell wall that is likely to hinder histone extraction. We report in this work a rapid and reliable method for extract

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Yu, Yucong, Hong Wen, and Xiaobing Shi. "Histone mimics: more tales to read." Biochemical Journal 478, no. 14 (2021): 2789–91. http://dx.doi.org/10.1042/bcj20210357.

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Post-translational modifications (PTMs) on histone proteins are known as epigenetic marks that demarcate the status of chromatin. These modifications are ‘read' by specific reader proteins, which in turn recruit additional factors to modulate chromatin accessibility and the activity of the underlying DNA. Accumulating evidence suggests that these modifications are not restricted solely to histones, many non-histone proteins may function in a similar way through mimicking the histones. In this commentary, we briefly discuss a systematic study of the discovery of histone H3 N-terminal mimicry pr

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Yang, Siyi, Yidong Sun, and Wei Yu. "HDACs and Their Inhibitors on Post-Translational Modifications: The Regulation of Cardiovascular Disease." Cells 14, no. 14 (2025): 1116. https://doi.org/10.3390/cells14141116.

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Cardiovascular diseases (CVD), such as myocardial hypertrophy, heart failure, atherosclerosis, and myocardial ischemia/reperfusion (I/R) injury, are among the major threats to human health worldwide. Post-translational modifications alter the function of proteins through dynamic chemical modification after synthesis. This mechanism not only plays an important role in maintaining homeostasis and plays a crucial role in maintaining normal cardiovascular function, but is also closely related to the pathological state of various diseases. Histone deacetylases (HDACs) play an important role in the

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Imbriano, Carol, and Silvia Belluti. "Histone Marks-Dependent Effect on Alternative Splicing: New Perspectives for Targeted Splicing Modulation in Cancer?" International Journal of Molecular Sciences 23, no. 15 (2022): 8304. http://dx.doi.org/10.3390/ijms23158304.

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Alternative splicing (AS) is a tightly regulated mechanism that generates the complex human proteome from a small number of genes. Cis-regulatory RNA motifs in exons and introns control AS, recruiting positive and negative trans-acting splicing regulators. At a higher level, chromatin affects splicing events. Growing evidence indicates that the popular histone code hypothesis can be extended to RNA-level processes, such as AS. In addition to nucleosome positioning, which can generate transcriptional barriers to shape the final splicing outcome, histone post-translational modifications can cont

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