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Journal articles on the topic 'Granules RNP'

Author: Grafiati

Published: 24 June 2021

Last updated: 5 February 2022

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1

Krüger, Timothy, Mario Hofweber, and Susanne Kramer. "SCD6 induces ribonucleoprotein granule formation in trypanosomes in a translation-independent manner, regulated by its Lsm and RGG domains." Molecular Biology of the Cell 24, no. 13 (2013): 2098–111. http://dx.doi.org/10.1091/mbc.e13-01-0068.

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Ribonucleoprotein (RNP) granules are cytoplasmic, microscopically visible structures composed of RNA and protein with proposed functions in mRNA decay and storage. Trypanosomes have several types of RNP granules, but lack most of the granule core components identified in yeast and humans. The exception is SCD6/Rap55, which is essential for processing body (P-body) formation. In this study, we analyzed the role of trypanosome SCD6 in RNP granule formation. Upon overexpression, the majority of SCD6 aggregates to multiple granules enriched at the nuclear periphery that recruit both P-body and str

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An, Haiyan, Jing Tong Tan, and Tatyana A. Shelkovnikova. "Stress granules regulate stress-induced paraspeckle assembly." Journal of Cell Biology 218, no. 12 (2019): 4127–40. http://dx.doi.org/10.1083/jcb.201904098.

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Eukaryotic cells contain a variety of RNA-protein macrocomplexes termed RNP granules. Different types of granules share multiple protein components; however, the crosstalk between spatially separated granules remains unaddressed. Paraspeckles and stress granules (SGs) are prototypical RNP granules localized exclusively in the nucleus and cytoplasm, respectively. Both granules are implicated in human diseases, such as amyotrophic lateral sclerosis. We characterized the composition of affinity-purified paraspeckle-like structures and found a significant overlap between the proteomes of paraspeck

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3

Hanazawa, Momoyo, Masafumi Yonetani, and Asako Sugimoto. "PGL proteins self associate and bind RNPs to mediate germ granule assembly in C. elegans." Journal of Cell Biology 192, no. 6 (2011): 929–37. http://dx.doi.org/10.1083/jcb.201010106.

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Germ granules are germ lineage–specific ribonucleoprotein (RNP) complexes, but how they are assembled and specifically segregated to germ lineage cells remains unclear. Here, we show that the PGL proteins PGL-1 and PGL-3 serve as the scaffold for germ granule formation in Caenorhabditis elegans. Using cultured mammalian cells, we found that PGL proteins have the ability to self-associate and recruit RNPs. Depletion of PGL proteins from early C. elegans embryos caused dispersal of other germ granule components in the cytoplasm, suggesting that PGL proteins are essential for the architecture of

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4

Davis, Michael, Andrea Montalbano, Megan P. Wood, and Jennifer A. Schisa. "Biphasic adaptation to osmotic stress in the C. elegans germ line." American Journal of Physiology-Cell Physiology 312, no. 6 (2017): C741—C748. http://dx.doi.org/10.1152/ajpcell.00364.2016.

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Cells respond to environmental stress in multiple ways. In the germ line, heat shock and nutritive stress trigger the assembly of large ribonucleoprotein (RNP) granules via liquid-liquid phase separation (LLPS). The RNP granules are hypothesized to maintain the quality of oocytes during stress. The goal of this study was to investigate the cellular response to glucose in the germ line and determine if it is an osmotic stress response. We found that exposure to 500 mM glucose induces the assembly of RNP granules in the germ line within 1 h. Interestingly, the RNP granules are maintained for up

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5

Aoki, Scott T., Aaron M. Kershner, Craig A. Bingman, Marvin Wickens, and Judith Kimble. "PGL germ granule assembly protein is a base-specific, single-stranded RNase." Proceedings of the National Academy of Sciences 113, no. 5 (2016): 1279–84. http://dx.doi.org/10.1073/pnas.1524400113.

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Cellular RNA-protein (RNP) granules are ubiquitous and have fundamental roles in biology and RNA metabolism, but the molecular basis of their structure, assembly, and function is poorly understood. Using nematode “P-granules” as a paradigm, we focus on the PGL granule scaffold protein to gain molecular insights into RNP granule structure and assembly. We first identify a PGL dimerization domain (DD) and determine its crystal structure. PGL-1 DD has a novel 13 α-helix fold that creates a positively charged channel as a homodimer. We investigate its capacity to bind RNA and discover unexpectedly

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Van Treeck, Briana, David S. W. Protter, Tyler Matheny, Anthony Khong, Christopher D. Link, and Roy Parker. "RNA self-assembly contributes to stress granule formation and defining the stress granule transcriptome." Proceedings of the National Academy of Sciences 115, no. 11 (2018): 2734–39. http://dx.doi.org/10.1073/pnas.1800038115.

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Stress granules are higher order assemblies of nontranslating mRNAs and proteins that form when translation initiation is inhibited. Stress granules are thought to form by protein–protein interactions of RNA-binding proteins. We demonstrate RNA homopolymers or purified cellular RNA forms assemblies in vitro analogous to stress granules. Remarkably, under conditions representative of an intracellular stress response, the mRNAs enriched in assemblies from total yeast RNA largely recapitulate the stress granule transcriptome. We suggest stress granules are formed by a summation of protein–protein

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An, Haiyan, and Tatyana A. Shelkovnikova. "Stress granules regulate paraspeckles: RNP granule continuum at work." Cell Stress 3, no. 12 (2019): 385–87. http://dx.doi.org/10.15698/cst2019.12.207.

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8

Noble, Scott L., Brittany L. Allen, Lai Kuan Goh, Kristen Nordick, and Thomas C. Evans. "Maternal mRNAs are regulated by diverse P body–related mRNP granules during early Caenorhabditis elegans development." Journal of Cell Biology 182, no. 3 (2008): 559–72. http://dx.doi.org/10.1083/jcb.200802128.

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Processing bodies (P bodies) are conserved mRNA–protein (mRNP) granules that are thought to be cytoplasmic centers for mRNA repression and degradation. However, their specific functions in vivo remain poorly understood. We find that repressed maternal mRNAs and their regulators localize to P body–like mRNP granules in the Caenorhabditis elegans germ line. Surprisingly, several distinct types of regulated granules form during oocyte and embryo development. 3′ untranslated region elements direct mRNA targeting to one of these granule classes. The P body factor CAR-1/Rap55 promotes association of

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9

De Graeve, Fabienne, and Florence Besse. "Neuronal RNP granules: from physiological to pathological assemblies." Biological Chemistry 399, no. 7 (2018): 623–35. http://dx.doi.org/10.1515/hsz-2018-0141.

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Abstract Neuronal cells rely on macro- and micro-cellular compartmentalization to rapidly process information, and respond locally to external stimuli. Such a cellular organization is achieved via the assembly of neuronal ribonucleoprotein (RNP) granules, dynamic membrane-less organelles enriched in RNAs and associated regulatory proteins. In this review, we discuss how these high-order structures transport mRNAs to dendrites and axons, and how they contribute to the spatio-temporal regulation of localized mRNA translation. We also highlight how recent biophysical studies have shed light on th

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10

Corbet, Giulia Ada, and Roy Parker. "RNP Granule Formation: Lessons from P-Bodies and Stress Granules." Cold Spring Harbor Symposia on Quantitative Biology 84 (2019): 203–15. http://dx.doi.org/10.1101/sqb.2019.84.040329.

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11

Burke, James M., Evan T. Lester, Devin Tauber, and Roy Parker. "RNase L promotes the formation of unique ribonucleoprotein granules distinct from stress granules." Journal of Biological Chemistry 295, no. 6 (2020): 1426–38. http://dx.doi.org/10.1074/jbc.ra119.011638.

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Stress granules (SGs) are ribonucleoprotein (RNP) assemblies that form in eukaryotic cells as a result of limited translation in response to stress. SGs form during viral infection and are thought to promote the antiviral response because many viruses encode inhibitors of SG assembly. However, the antiviral endoribonuclease RNase L also alters SG formation, whereby only small punctate SG-like bodies that we term RNase L–dependent bodies (RLBs) form during RNase L activation. How RLBs relate to SGs and their mode of biogenesis is unknown. Herein, using immunofluorescence, live-cell imaging, and

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12

Yasuda, Kyota, Huaye Zhang, David Loiselle, Timothy Haystead, Ian G. Macara, and Stavroula Mili. "The RNA-binding protein Fus directs translation of localized mRNAs in APC-RNP granules." Journal of Cell Biology 203, no. 5 (2013): 737–46. http://dx.doi.org/10.1083/jcb.201306058.

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RNA localization pathways direct numerous mRNAs to distinct subcellular regions and affect many physiological processes. In one such pathway the tumor-suppressor protein adenomatous polyposis coli (APC) targets RNAs to cell protrusions, forming APC-containing ribonucleoprotein complexes (APC-RNPs). Here, we show that APC-RNPs associate with the RNA-binding protein Fus/TLS (fused in sarcoma/translocated in liposarcoma). Fus is not required for APC-RNP localization but is required for efficient translation of associated transcripts. Labeling of newly synthesized proteins revealed that Fus promot

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13

Hubstenberger, Arnaud, Cristiana Cameron, Scott L. Noble, Sean Keenan, and Thomas C. Evans. "Modifiers of solid RNP granules control normal RNP dynamics and mRNA activity in early development." Journal of Cell Biology 211, no. 3 (2015): 703–16. http://dx.doi.org/10.1083/jcb.201504044.

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Ribonucleoproteins (RNPs) often coassemble into supramolecular bodies with regulated dynamics. The factors controlling RNP bodies and connections to RNA regulation are unclear. During Caenorhabditis elegans oogenesis, cytoplasmic RNPs can transition among diffuse, liquid, and solid states linked to mRNA regulation. Loss of CGH-1/Ddx6 RNA helicase generates solid granules that are sensitive to mRNA regulators. Here, we identified 66 modifiers of RNP solids induced by cgh-1 mutation. A majority of genes promote or suppress normal RNP body assembly, dynamics, or metabolism. Surprisingly, polyaden

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14

Rhine, Kevin, Velinda Vidaurre, and Sua Myong. "RNA Droplets." Annual Review of Biophysics 49, no. 1 (2020): 247–65. http://dx.doi.org/10.1146/annurev-biophys-052118-115508.

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Liquid–liquid phase separation is emerging as the universal mechanism by which membraneless cellular granules form. Despite many previous studies on condensation of intrinsically disordered proteins and low complexity domains, we lack understanding about the role of RNA, which is the essential component of all ribonucleoprotein (RNP) granules. RNA, as an anionic polymer, is inherently an excellent platform for achieving multivalency and can accommodate many RNA binding proteins. Recent findings have highlighted the diverse function of RNA in tuning phase-separation propensity up or down, alter

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15

Short, Ben. "Solidifying the view of RNP dynamics." Journal of Cell Biology 211, no. 3 (2015): 487. http://dx.doi.org/10.1083/jcb.2113if.

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16

Lehtiniemi, Tiina, and Noora Kotaja. "Germ granule-mediated RNA regulation in male germ cells." Reproduction 155, no. 2 (2018): R77—R91. http://dx.doi.org/10.1530/rep-17-0356.

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Germ cells have exceptionally diverse transcriptomes. Furthermore, the progress of spermatogenesis is accompanied by dramatic changes in gene expression patterns, the most drastic of them being near-to-complete transcriptional silencing during the final steps of differentiation. Therefore, accurate RNA regulatory mechanisms are critical for normal spermatogenesis. Cytoplasmic germ cell-specific ribonucleoprotein (RNP) granules, known as germ granules, participate in posttranscriptional regulation in developing male germ cells. Particularly, germ granules provide platforms for the PIWI-interact

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17

Rao, Bhalchandra S., and Roy Parker. "Numerous interactions act redundantly to assemble a tunable size of P bodies in Saccharomyces cerevisiae." Proceedings of the National Academy of Sciences 114, no. 45 (2017): E9569—E9578. http://dx.doi.org/10.1073/pnas.1712396114.

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Eukaryotic cells contain multiple RNA–protein assemblies referred to as RNP granules, which are thought to form through multiple protein–protein interactions analogous to a liquid–liquid phase separation. One class of RNP granules consists of P bodies, which consist of nontranslating mRNAs and the general translation repression and mRNA degradation machinery. P bodies have been suggested to form predominantly through interactions of Edc3 and a prion-like domain on Lsm4. In this work, we provide evidence that P-body assembly can be driven by multiple different protein–protein and/or protein–RNA

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18

ABOLHASSANI-DADRAS, S., G. H. VÁZQUEZ-NIN, O. M. ECHEVERRÍA, V. BOUTINARD ROUELLE-ROSSIER, and S. FAKAN. "ESI in situ analyses of extrachromosomal RNP granules." Journal of Microscopy 174, no. 3 (1994): 233–38. http://dx.doi.org/10.1111/j.1365-2818.1994.tb03470.x.

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19

Glätzer, K. H., and P. M. Kloetzel. "Differential chromosomal distribution of ribonucleoprotein antigens in nuclei of Drosophila spermatocytes." Journal of Cell Biology 103, no. 6 (1986): 2113–19. http://dx.doi.org/10.1083/jcb.103.6.2113.

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The ribonucleoprotein (RNP) composition of the active Y chromosomal structures in spermatocyte nuclei of Drosophila hydei has been investigated using the anti-RNP antibodies Dm 28K2 and pp60 as a probe. Antibody Dm 28K2 was raised against an RNP protein of cytoplasmic RNP particles in D. melanogaster cells, while antibody pp60 was raised against a pre-messenger RNP fraction from oocytes of Xenopus laevis. Both antibodies detect nuclear RNP (nRNP) antigens of D. hydei. This is shown by CsCl density centrifugation of nRNP from D. hydei cells and immunoblotting across the density gradient. Dm 28K

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20

Abolhassani-Dadras, S., G. H. Vázquez-Nin, O. M. Echeverría, and S. Fakan. "The use of an internal standard in the application of quantitative image-EELS in biology." Proceedings, annual meeting, Electron Microscopy Society of America 54 (August 11, 1996): 50–51. http://dx.doi.org/10.1017/s0424820100162715.

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The energy filtering transmission electron microscope (EFTEM) is employed to examine the possibility of using ribosomes as internal standard for a quantitative in-situ study of phosphorus content of nuclear constituents in a biological section. The problems that can arise from different steps of such an experimental approach are discussed.Salivary gland cells from fourth instar larvae of Chironomus thummi are selected as test specimens because of their appropriate structure. The nucleus of these cells contains two types of granules, one of which (known as Balbiani ring granule, Brg) has an RNA

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21

Biggiogera, Marco, Maria Grazia Bottone, and Carlo Pellicciari. "Nuclear RNA Is Extruded from Apoptotic Cells." Journal of Histochemistry & Cytochemistry 46, no. 9 (1998): 999–1005. http://dx.doi.org/10.1177/002215549804600903.

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During spontaneous apoptosis of thymocytes there is extrusion of ribonucleoproteins (RNPs) from the cell. The aim of this investigation was to elucidate whether the RNP aggregates in apoptotic cells and bodies still contain RNA in an appreciable amount. We demonstrated by specific cytochemical techniques that the aggregates of nuclear RNPs extruded in the cytoplasm of spontaneously apoptotic thymocytes contain RNA in a sufficient amount to be detected cytochemically. These heterogeneous ectopic RNP-derived structures (HERDS) are formed by perichromatin fibrils, interchromatin granules, perichr

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22

Goodier, John L., Lili Zhang, Melissa R. Vetter, and Haig H. Kazazian. "LINE-1 ORF1 Protein Localizes in Stress Granules with Other RNA-Binding Proteins, Including Components of RNA Interference RNA-Induced Silencing Complex." Molecular and Cellular Biology 27, no. 18 (2007): 6469–83. http://dx.doi.org/10.1128/mcb.00332-07.

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ABSTRACT LINE-1 retrotransposons constitute one-fifth of human DNA and have helped shape our genome. A full-length L1 encodes a 40-kDa RNA-binding protein (ORF1p) and a 150-kDa protein (ORF2p) with endonuclease and reverse transcriptase activities. ORF1p is distinctive in forming large cytoplasmic foci, which we identified as cytoplasmic stress granules. A phylogenetically conserved central region of the protein is critical for wild-type localization and retrotransposition. Yeast two-hybrid screens revealed several RNA-binding proteins that coimmunoprecipitate with ORF1p and colocalize with OR

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23

Standart, Nancy, and Nicola Minshall. "Translational control in early development: CPEB, P-bodies and germinal granules." Biochemical Society Transactions 36, no. 4 (2008): 671–76. http://dx.doi.org/10.1042/bst0360671.

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Selective protein synthesis in oocytes, eggs and early embryos of many organisms drives several critical aspects of early development, including meiotic maturation and entry into mitosis, establishment of embryonic axes and cell fate determination. mRNA-binding proteins which (usually) recognize 3′-UTR (untranslated region) elements in target mRNAs influence the recruitment of the small ribosomal subunit to the 5′ cap. Probably the best studied such protein is CPEB (cytoplasmic polyadenylation element-binding protein), which represses translation in the oocyte in a cap-dependent manner, and ac

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Zhang, Yi, Jiayu Gu, and Qiming Sun. "Aberrant Stress Granule Dynamics and Aggrephagy in ALS Pathogenesis." Cells 10, no. 9 (2021): 2247. http://dx.doi.org/10.3390/cells10092247.

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Stress granules are conserved cytosolic ribonucleoprotein (RNP) compartments that undergo dynamic assembly and disassembly by phase separation in response to stressful conditions. Gene mutations may lead to aberrant phase separation of stress granules eliciting irreversible protein aggregations. A selective autophagy pathway called aggrephagy may partially alleviate the cytotoxicity mediated by these protein aggregates. Cells must perceive when and where the stress granules are transformed into toxic protein aggregates to initiate autophagosomal engulfment for subsequent autolysosomal degradat

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Nielsen, Finn C., Jacob Nielsen, Mette A. Kristensen, Grete Koch, and Jan Christiansen. "Cytoplasmic trafficking of IGF-II mRNA-binding protein by conserved KH domains." Journal of Cell Science 115, no. 10 (2002): 2087–97. http://dx.doi.org/10.1242/jcs.115.10.2087.

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The IGF-II mRNA-binding proteins (IMPs), which are composed of two RNA recognition motifs, (RRM) and four hnRNP K homology (KH) domains, have been implicated in subcytoplasmic localization of mRNAs during embryogenesis. The IMP family originated via two gene duplications before the divergence of vertebrates, and IMP homologues consisting of only the four KH motifs have been identified in Drosophila and Caenorhabditis elegans. Here we characterise the trafficking of GFP-IMP1 fusion proteins and determine the structural determinants for proper cytoplasmic localization. GFP-IMP1 is present in lar

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Desai, Perlina, and Rina Bandopadhyay. "Pathophysiological implications of RNP granules in frontotemporal dementia and ALS." Neurochemistry International 140 (November 2020): 104819. http://dx.doi.org/10.1016/j.neuint.2020.104819.

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27

Moon, Stephanie L., Tatsuya Morisaki, Anthony Khong, Kenneth Lyon, Roy Parker, and Timothy J. Stasevich. "Multicolour single-molecule tracking of mRNA interactions with RNP granules." Nature Cell Biology 21, no. 2 (2019): 162–68. http://dx.doi.org/10.1038/s41556-018-0263-4.

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Wurtz-T, E. Kiseleva, G. Nacheva, A. Alzhanova-Ericcson, A. Rosén, and B. Daneholt. "Identification of two RNA-binding proteins in Balbiani ring premessenger ribonucleoprotein granules and presence of these proteins in specific subsets of heterogeneous nuclear ribonucleoprotein particles." Molecular and Cellular Biology 16, no. 4 (1996): 1425–35. http://dx.doi.org/10.1128/mcb.16.4.1425.

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Balbiani ring (BR) granules are premessenger ribonucleoprotein particles (RNPs) generated in giant chromosomal puffs, the BRs, in the larval salivary glands of the dipteran chironomus tentans. Monoclonal antibodies were raised against nuclear proteins collected on a single-stranded-DNA-agarose affinity column, and two of them were used to identify RNA-binding proteins in BR granules. First, in Western blots (immunoblots), one of the antibodies recognized a 36-kDa protein and the other recognized a 45-KDa protein. Second, both antibodies bound to the BRs in immunocytological experiments. It was

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Cambray, Serafí, Neus Pedraza, Marta Rafel, Eloi Garí, Martí Aldea, and Carme Gallego. "Protein Kinase KIS Localizes to RNA Granules and Enhances Local Translation." Molecular and Cellular Biology 29, no. 3 (2008): 726–35. http://dx.doi.org/10.1128/mcb.01180-08.

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ABSTRACT The regulation of mRNA transport is a fundamental process for cytoplasmic sorting of transcripts and spatially controlled translational derepression once properly localized. There is growing evidence that translation is locally modulated as a result of specific synaptic inputs. However, the underlying molecular mechanisms that regulate this translational process are just emerging. We show that KIS, a serine/threonine kinase functionally related to microtubule dynamics and axon development, interacts with three proteins found in RNA granules: KIF3A, NonO, and eEF1A. KIS localizes to RN

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Pizzinga, Mariavittoria, Christian Bates, Jennifer Lui, et al. "Translation factor mRNA granules direct protein synthetic capacity to regions of polarized growth." Journal of Cell Biology 218, no. 5 (2019): 1564–81. http://dx.doi.org/10.1083/jcb.201704019.

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mRNA localization serves key functions in localized protein production, making it critical that the translation machinery itself is present at these locations. Here we show that translation factor mRNAs are localized to distinct granules within yeast cells. In contrast to many messenger RNP granules, such as processing bodies and stress granules, which contain translationally repressed mRNAs, these granules harbor translated mRNAs under active growth conditions. The granules require Pab1p for their integrity and are inherited by developing daughter cells in a She2p/She3p-dependent manner. Thes

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Semeshin, V. F., I. F. Zhimulev, D. Kritikou, and A. Zacharopoulou. "Electron microscope investigation of polytene chromosomes in the Mediterranean fruit fly Ceratitis capitata." Genome 38, no. 4 (1995): 652–60. http://dx.doi.org/10.1139/g95-083.

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Ultrastructural analyses of polytene chromosomes from male pupal orbital bristle cells and from larval salivary glands of Ceratitis capitata were carried out. It was shown that chromatin complexes corresponding to the X chromosome heterochromatic network are surrounded by material containing ribonucleoprotein (RNP) granules 250–300 Å (1 Å = 0.1 nm) in diameter. RNP granules of similar size surround the spherical Y chromosome. These data point out the presence of transcriptional activity in both of these chromosomes. The absence of clear structure in chromosomal regions situated between large b

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Kaur, Taranpreet, Ibraheem Alshareedah, Wei Wang, Jason Ngo, Mahdi Moosa, and Priya Banerjee. "Molecular Crowding Tunes Material States of Ribonucleoprotein Condensates." Biomolecules 9, no. 2 (2019): 71. http://dx.doi.org/10.3390/biom9020071.

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Ribonucleoprotein (RNP) granules are membraneless liquid condensates that dynamically form, dissolve, and mature into a gel-like state in response to a changing cellular environment. RNP condensation is largely governed by promiscuous attractive inter-chain interactions mediated by low-complexity domains (LCDs). Using an archetypal disordered RNP, fused in sarcoma (FUS), here we study how molecular crowding impacts the RNP liquid condensation. We observe that the liquid–liquid coexistence boundary of FUS is lowered by polymer crowders, consistent with an excluded volume model. With increasing

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Olins, Ada L., Donald E. Olins, Manesh B. Shah, Henri A. Levy, and David P. Bazett-Jonest. "The 3-D substructure of RNA in nascent RNP granules: A novel application of osmium ammine-B staining and electron spectroscopic imaging." Proceedings, annual meeting, Electron Microscopy Society of America 50, no. 1 (1992): 504–5. http://dx.doi.org/10.1017/s0424820100122927.

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RNA has a particulate substructure when visualized in situ with the nucleic acid specific stain osmium ammine-B (OA-B). In this study energy spectroscopic imaging (ESI) was used to enhance the contrast and collect the data for tomographic reconstructions.The Balbiani ring (BR) in the salivary gland polytene chromosomes of Chironomus tentans larvae furnishes a well known model for the structure of nascent m-RNA. This gland produces copious amounts of silk-like secretory proteins which are very large (106 daltons). The site of transcription, the BR, is easily recognized in the EM by its characte

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Iwaki, Aya, Takao Kawai, Yosuke Yamamoto, and Shingo Izawa. "Biomass Conversion Inhibitors Furfural and 5-Hydroxymethylfurfural Induce Formation of Messenger RNP Granules and Attenuate Translation Activity in Saccharomyces cerevisiae." Applied and Environmental Microbiology 79, no. 5 (2012): 1661–67. http://dx.doi.org/10.1128/aem.02797-12.

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ABSTRACTVarious forms of stress can cause an attenuation of bulk translation activity and the accumulation of nontranslating mRNAs into cytoplasmic messenger RNP (mRNP) granules termed processing bodies (P-bodies) and stress granules (SGs) in eukaryotic cells. Furfural and 5-hydroxymethylfurfural (HMF), derived from lignocellulosic biomass, inhibit yeast growth and fermentation as stressors. Since there is no report regarding their effects on the formation of cytoplasmic mRNP granules, here we investigated whether furfural and HMF cause the assembly of yeast P-bodies and SGs accompanied by tra

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Soop, Teresa, Birgitta Ivarsson, Birgitta Björkroth, et al. "Nup153 Affects Entry of Messenger and Ribosomal Ribonucleoproteins into the Nuclear Basket during Export." Molecular Biology of the Cell 16, no. 12 (2005): 5610–20. http://dx.doi.org/10.1091/mbc.e05-08-0715.

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A specific messenger ribonucleoprotein (RNP) particle, Balbiani ring (BR) granules in the dipteran Chironomus tentans, can be visualized during passage through the nuclear pore complex (NPC). We have now examined the transport through the nuclear basket preceding the actual translocation through the NPC. The basket consists of eight fibrils anchored to the NPC core by nucleoprotein Nup153. On nuclear injection of anti-Nup153, the transport of BR granules is blocked. Many granules are retained on top of the nuclear basket, whereas no granules are seen in transit through NPC. Interestingly, the

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Naarmann, I. S., C. Harnisch, G. Muller-Newen, H. Urlaub, A. Ostareck-Lederer, and D. H. Ostareck. "DDX6 recruits translational silenced human reticulocyte 15-lipoxygenase mRNA to RNP granules." RNA 16, no. 11 (2010): 2189–204. http://dx.doi.org/10.1261/rna.2211110.

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37

Krüger, Tim, Hanswalter Zentgraf, and Ulrich Scheer. "Intranucleolar sites of ribosome biogenesis defined by the localization of early binding ribosomal proteins." Journal of Cell Biology 177, no. 4 (2007): 573–78. http://dx.doi.org/10.1083/jcb.200612048.

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Considerable efforts are being undertaken to elucidate the processes of ribosome biogenesis. Although various preribosomal RNP complexes have been isolated and molecularly characterized, the order of ribosomal protein (r-protein) addition to the emerging ribosome subunits is largely unknown. Furthermore, the correlation between the ribosome assembly pathway and the structural organization of the dedicated ribosome factory, the nucleolus, is not well established. We have analyzed the nucleolar localization of several early binding r-proteins in human cells, applying various methods, including l

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Aronov, Stella, Saray Dover-Biterman, Edith Suss-Toby, Michael Shmoish, Lea Duek, and Mordechai Choder. "Pheromone-encoding mRNA is transported to the yeast mating projection by specific RNP granules." Journal of Cell Biology 209, no. 6 (2015): 829–42. http://dx.doi.org/10.1083/jcb.201408045.

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Association of messenger RNAs with large complexes such as processing bodies (PBs) plays a pivotal role in regulating their translation and decay. Little is known about other possible functions of these assemblies. Exposure of haploid yeast cells, carrying mating type “a,” to “α pheromone” stimulates polarized growth resulting in a “shmoo” projection; it also induces synthesis of “a pheromone,” encoded by MFA2. In this paper, we show that, in response to α pheromone, MFA2 mRNA is assembled with two types of granules; both contain some canonical PB proteins, yet they differ in size, localizatio

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Kato, Yasuko, and Akira Nakamura. "Roles of cytoplasmic RNP granules in intracellular RNA localization and translational control in the Drosophila oocyte." Development, Growth & Differentiation 54, no. 1 (2011): 19–31. http://dx.doi.org/10.1111/j.1440-169x.2011.01314.x.

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Bhatter, Nupur, Rajan Iyyappan, Gayatri Mohanan, and Purusharth I. Rajyaguru. "Exploring the role of RRM domains and conserved aromatic residues in RGG motif of eIF4G-binding translation repressor protein Sbp1." Wellcome Open Research 3 (September 17, 2021): 102. http://dx.doi.org/10.12688/wellcomeopenres.14709.3.

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Background: RNA binding proteins play crucial role in determining if a given mRNA will be translated, stored, or degraded. Sbp1 is an RGG-motif containing protein that is implicated in affecting mRNA decapping and translation. Sbp1 represses translation by binding eIF4G1 through its RGG-motif and activates decapping when overexpressed. In this report, we have assessed the genetic interaction of Sbp1 with decapping activators such as Dhh1, Pat1, and Scd6. We have further analyzed the importance of different domains and specific conserved residues of Sbp1 in its ability to cause over-expression

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ABOLHAS SANI-DADRAS, S., G. H. VÁZQUEZ-NIN, O. M. ECHEVERRÍA, and S. FAKAN. "Image-EELS for in situ estimation of the phosphorus content of RNP granules." Journal of Microscopy 183, no. 3 (1996): 215–22. http://dx.doi.org/10.1046/j.1365-2818.1996.950653.x.

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Ling, Shuo-Chien. "Synaptic Paths to Neurodegeneration: The Emerging Role of TDP-43 and FUS in Synaptic Functions." Neural Plasticity 2018 (2018): 1–13. http://dx.doi.org/10.1155/2018/8413496.

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TAR DNA-binding protein-43 KDa (TDP-43) and fused in sarcoma (FUS) as the defining pathological hallmarks for amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), coupled with ALS-FTD-causing mutations in both genes, indicate that their dysfunctions damage the motor system and cognition. On the molecular level, TDP-43 and FUS participate in the biogenesis and metabolism of coding and noncoding RNAs as well as in the transport and translation of mRNAs as part of cytoplasmic mRNA-ribonucleoprotein (mRNP) granules. Intriguingly, many of the RNA targets of TDP-43 and FUS are invo

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Ravanidis, Stylianos, Fedon-Giasin Kattan, and Epaminondas Doxakis. "Unraveling the Pathways to Neuronal Homeostasis and Disease: Mechanistic Insights into the Role of RNA-Binding Proteins and Associated Factors." International Journal of Molecular Sciences 19, no. 8 (2018): 2280. http://dx.doi.org/10.3390/ijms19082280.

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The timing, dosage and location of gene expression are fundamental determinants of brain architectural complexity. In neurons, this is, primarily, achieved by specific sets of trans-acting RNA-binding proteins (RBPs) and their associated factors that bind to specific cis elements throughout the RNA sequence to regulate splicing, polyadenylation, stability, transport and localized translation at both axons and dendrites. Not surprisingly, misregulation of RBP expression or disruption of its function due to mutations or sequestration into nuclear or cytoplasmic inclusions have been linked to the

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Bhatter, Nupur, Rajan Iyyappan, and Purusharth I. Rajyaguru. "Exploring the role of RRM domains and conserved aromatic residues in RGG motif of eIF4G-binding translation repressor protein Sbp1." Wellcome Open Research 3 (February 6, 2020): 102. http://dx.doi.org/10.12688/wellcomeopenres.14709.2.

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Background: Mechanisms of mRNA fate decisions play an important role in determining if a given mRNA will be translated, stored or degraded upon arrival to cytoplasm. Sbp1 is an important RGG-motif containing protein that is implicated in affecting mRNA decapping and translation. Sbp1 represses translation by binding eIF4G1 through its RGG-motif and activates decapping when overexpressed. In this report we have assessed the genetic interaction of Sbp1 with decapping activators such as Dhh1, Pat1 and Scd6. We have further analyzed the importance of different domains and specific conserved residu

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Wood, Megan P., Angela Hollis, Ashley L. Severance, Megan L. Karrick, and Jennifer A. Schisa. "RNAi Screen Identifies Novel Regulators of RNP Granules in the Caenorhabditis elegans Germ Line." G3: Genes|Genomes|Genetics 6, no. 8 (2016): 2643–54. http://dx.doi.org/10.1534/g3.116.031559.

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Ivanov, P. A., and E. S. Nadezhdina. "Stress granules: RNP-containing cytoplasmic bodies arising in stress: Structure and mechanism of organization." Molecular Biology 40, no. 6 (2006): 844–50. http://dx.doi.org/10.1134/s0026893306060021.

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Gallois-Montbrun, Sarah, Beatrice Kramer, Chad M. Swanson, et al. "Antiviral Protein APOBEC3G Localizes to Ribonucleoprotein Complexes Found in P Bodies and Stress Granules." Journal of Virology 81, no. 5 (2006): 2165–78. http://dx.doi.org/10.1128/jvi.02287-06.

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ABSTRACT Members of the APOBEC (apolipoprotein B mRNA-editing enzyme catalytic polypeptide 1-like) family of cytidine deaminases inhibit host cell genome invasion by exogenous retroviruses and endogenous retrotransposons. Because these enzymes can edit DNA or RNA and potentially mutate cellular targets, their activities are presumably regulated; for instance, APOBEC3G (A3G) recruitment into high-molecular-weight ribonucleoprotein (RNP) complexes has been shown to suppress its enzymatic activity. We used tandem affinity purification together with mass spectrometry (MS) to identify protein compo

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Fritz, Melanie, Jens Vanselow, Nadja Sauer, et al. "Novel insights into RNP granules by employing the trypanosome's microtubule skeleton as a molecular sieve." Nucleic Acids Research 43, no. 16 (2015): 8013–32. http://dx.doi.org/10.1093/nar/gkv731.

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Jonas, S., and E. Izaurralde. "The role of disordered protein regions in the assembly of decapping complexes and RNP granules." Genes & Development 27, no. 24 (2013): 2628–41. http://dx.doi.org/10.1101/gad.227843.113.

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Rojas, Marta, George W. Farr, Cesar F. Fernandez, Laura Lauden, John C. McCormack, and Sandra L. Wolin. "Yeast Gis2 and Its Human Ortholog CNBP Are Novel Components of Stress-Induced RNP Granules." PLoS ONE 7, no. 12 (2012): e52824. http://dx.doi.org/10.1371/journal.pone.0052824.

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