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Journal articles on the topic 'Complexes PRC2'

Author: Grafiati

Published: 4 June 2021

Last updated: 14 February 2022

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1

Majewski, Ian J., Matthew E. Ritchie, Belinda Phipson, et al. "Opposing roles of polycomb repressive complexes in hematopoietic stem and progenitor cells." Blood 116, no. 5 (2010): 731–39. http://dx.doi.org/10.1182/blood-2009-12-260760.

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Polycomb group (PcG) proteins are transcriptional repressors with a central role in the establishment and maintenance of gene expression patterns during development. We have investigated the role of polycomb repressive complexes (PRCs) in hematopoietic stem cells (HSCs) and progenitor populations. We show that mice with loss of function mutations in PRC2 components display enhanced HSC/progenitor population activity, whereas mutations that disrupt PRC1 or pleiohomeotic repressive complex are associated with HSC/progenitor cell defects. Because the hierarchical model of PRC action would predict

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2

Sharma, Adhikarimayum Lakhikumar, Joseph Hokello, Shilpa Sonti, et al. "CBF-1 Promotes the Establishment and Maintenance of HIV Latency by Recruiting Polycomb Repressive Complexes, PRC1 and PRC2, at HIV LTR." Viruses 12, no. 9 (2020): 1040. http://dx.doi.org/10.3390/v12091040.

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The C-promoter binding factor-1 (CBF-1) is a potent and specific inhibitor of the human immunodeficiency virus (HIV)-1 LTR promoter. Here, we demonstrate that the knockdown of endogenous CBF-1 in latently infected primary CD4+ T cells, using specific small hairpin RNAs (shRNA), resulted in the reactivation of latent HIV proviruses. Chromatin immunoprecipitation (ChIP) assays using latently infected primary T cells and Jurkat T-cell lines demonstrated that CBF-1 induces the establishment and maintenance of HIV latency by recruiting polycomb group (PcG/PRC) corepressor complexes or polycomb repr

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3

Hinsch, Valerie, Samuel Adkins, Darren Manuela, and Mingli Xu. "Post-Embryonic Phase Transitions Mediated by Polycomb Repressive Complexes in Plants." International Journal of Molecular Sciences 22, no. 14 (2021): 7533. http://dx.doi.org/10.3390/ijms22147533.

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Correct timing of developmental phase transitions is critical for the survival and fitness of plants. Developmental phase transitions in plants are partially promoted by controlling relevant genes into active or repressive status. Polycomb Repressive Complex1 (PRC1) and PRC2, originally identified in Drosophila, are essential in initiating and/or maintaining genes in repressive status to mediate developmental phase transitions. Our review summarizes mechanisms in which the embryo-to-seedling transition, the juvenile-to-adult transition, and vegetative-to-reproductive transition in plants are m

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4

Zepeda-Martinez, J. A., C. Pribitzer, J. Wang, et al. "Parallel PRC2/cPRC1 and vPRC1 pathways silence lineage-specific genes and maintain self-renewal in mouse embryonic stem cells." Science Advances 6, no. 14 (2020): eaax5692. http://dx.doi.org/10.1126/sciadv.aax5692.

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The transcriptional repressors Polycomb repressive complex 1 (PRC1) and PRC2 are required to maintain cell fate during embryonic development. PRC1 and PRC2 catalyze distinct histone modifications, establishing repressive chromatin at shared targets. How PRC1, which consists of canonical PRC1 (cPRC1) and variant PRC1 (vPRC1) complexes, and PRC2 cooperate to silence genes and support mouse embryonic stem cell (mESC) self-renewal is unclear. Using combinatorial genetic perturbations, we show that independent pathways of cPRC1 and vPRC1 are responsible for maintenance of H2A monoubiquitylation and

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5

Wang, Qiannan, and Wen-Hui Shen. "Chromatin modulation and gene regulation in plants: insight about PRC1 function." Biochemical Society Transactions 46, no. 4 (2018): 957–66. http://dx.doi.org/10.1042/bst20170576.

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In plant and metazoan, Polycomb Group (PcG) proteins play key roles in regulating developmental processes by repression of gene expression. PcG proteins function as multi-protein complexes; among them the best characterized ones are Polycomb Repressive Complex 1 (PRC1) and PRC2. PRC2 catalyzes histone H3 lysine 27 trimethylation (H3K27me3), and PRC1 can bind H3K27me3 and catalyzes H2A monoubiquitination. While the PRC2 components and molecular functions are evolutionarily conserved, varied PRC1 complexes are found and they show high divergences between animals and plants. In addition to the co

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6

Baile, Fernando, Wiam Merini, Inés Hidalgo, and Myriam Calonje. "EAR domain-containing transcription factors trigger PRC2-mediated chromatin marking in Arabidopsis." Plant Cell 33, no. 8 (2021): 2701–15. http://dx.doi.org/10.1093/plcell/koab139.

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Abstract Polycomb group (PcG) complexes ensure that every cell in an organism expresses the genes needed at a particular stage, time, or condition. However, it is still not fully understood how PcG complexes PcG-repressive complex 1 (PRC1) and PRC2 are recruited to target genes in plants. Recent findings in Arabidopsis thaliana support the notion that PRC2 recruitment is mediated by different transcription factors (TFs). However, it is unclear how all these TFs interact with PRC2 and whether they also recruit PRC1 activity. Here, by using a system to bind selected TFs to a synthetic promoter l

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7

Chittock, Emily C., Sebastian Latwiel, Thomas C. R. Miller, and Christoph W. Müller. "Molecular architecture of polycomb repressive complexes." Biochemical Society Transactions 45, no. 1 (2017): 193–205. http://dx.doi.org/10.1042/bst20160173.

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The polycomb group (PcG) proteins are a large and diverse family that epigenetically repress the transcription of key developmental genes. They form three broad groups of polycomb repressive complexes (PRCs) known as PRC1, PRC2 and Polycomb Repressive DeUBiquitinase, each of which modifies and/or remodels chromatin by distinct mechanisms that are tuned by having variable compositions of core and accessory subunits. Until recently, relatively little was known about how the various PcG proteins assemble to form the PRCs; however, studies by several groups have now allowed us to start piecing tog

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8

Brockdorff, Neil. "Polycomb complexes in X chromosome inactivation." Philosophical Transactions of the Royal Society B: Biological Sciences 372, no. 1733 (2017): 20170021. http://dx.doi.org/10.1098/rstb.2017.0021.

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Identifying the critical RNA binding proteins (RBPs) that elicit Xist mediated silencing has been a key goal in X inactivation research. Early studies implicated the Polycomb proteins, a family of factors linked to one of two major multiprotein complexes, PRC1 and PRC2 (Wang 2001 Nat. Genet. 28 , 371–375 ( doi:10.1038/ng574 ); Silva 2003 Dev. Cell 4 , 481–495 ( doi:10.1016/S1534-5807(03)00068-6 ); de Napoles 2004 Dev. Cell 7 , 663–676 ( doi:10.1016/j.devcel.2004.10.005 ); Plath 2003 Science 300 , 131–135 ( doi:10.1126/science.1084274 )). PRC1 and PRC2 complexes catalyse specific histone post-t

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9

Wang, Liangjun, Neal Jahren, Ellen L. Miller, Carrie S. Ketel, Daniel R. Mallin, and Jeffrey A. Simon. "Comparative Analysis of Chromatin Binding by Sex Comb on Midleg (SCM) and Other Polycomb Group Repressors at a Drosophila Hox Gene." Molecular and Cellular Biology 30, no. 11 (2010): 2584–93. http://dx.doi.org/10.1128/mcb.01451-09.

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ABSTRACT Sex Comb on Midleg (SCM) is a transcriptional repressor in the Polycomb group (PcG), but its molecular role in PcG silencing is not known. Although SCM can interact with Polycomb repressive complex 1 (PRC1) in vitro, biochemical studies have indicated that SCM is not a core constituent of PRC1 or PRC2. Nevertheless, SCM is just as critical for Drosophila Hox gene silencing as canonical subunits of these well-characterized PcG complexes. To address functional relationships between SCM and other PcG components, we have performed chromatin immunoprecipitation studies using cultured Droso

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10

Plath, Kathrin, Dale Talbot, Karien M. Hamer, et al. "Developmentally regulated alterations in Polycomb repressive complex 1 proteins on the inactive X chromosome." Journal of Cell Biology 167, no. 6 (2004): 1025–35. http://dx.doi.org/10.1083/jcb.200409026.

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Polycomb group (PcG) proteins belonging to the polycomb (Pc) repressive complexes 1 and 2 (PRC1 and PRC2) maintain homeotic gene silencing. In Drosophila, PRC2 methylates histone H3 on lysine 27, and this epigenetic mark facilitates recruitment of PRC1. Mouse PRC2 (mPRC2) has been implicated in X inactivation, as mPRC2 proteins transiently accumulate on the inactive X chromosome (Xi) at the onset of X inactivation to methylate histone H3 lysine 27 (H3-K27). In this study, we demonstrate that mPRC1 proteins localize to the Xi, and that different mPRC1 proteins accumulate on the Xi during initia

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11

Lin, Xingcheng, Rachel Leicher, Shixin Liu, and Bin Zhang. "Cooperative DNA looping by PRC2 complexes." Nucleic Acids Research 49, no. 11 (2021): 6238–48. http://dx.doi.org/10.1093/nar/gkab441.

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Abstract Polycomb repressive complex 2 (PRC2) is an essential protein complex that silences gene expression via post-translational modifications of chromatin. This paper combined homology modeling, atomistic and coarse-grained molecular dynamics simulations, and single-molecule force spectroscopy experiments to characterize both its full-length structure and PRC2-DNA interactions. Using free energy calculations with a newly parameterized protein-DNA force field, we studied a total of three potential PRC2 conformations and their impact on DNA binding and bending. Consistent with cryo-EM studies

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12

Yan, Bowen, Yanpeng Lv, Chunyu Zhao, and Xiaoxue Wang. "Knowing When to Silence: Roles of Polycomb-Group Proteins in SAM Maintenance, Root Development, and Developmental Phase Transition." International Journal of Molecular Sciences 21, no. 16 (2020): 5871. http://dx.doi.org/10.3390/ijms21165871.

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Polycomb repressive complex 1 (PRC1) and PRC2 are the major complexes composed of polycomb-group (PcG) proteins in plants. PRC2 catalyzes trimethylation of lysine 27 on histone 3 to silence target genes. Like Heterochromatin Protein 1/Terminal Flower 2 (LHP1/TFL2) recognizes and binds to H3K27me3 generated by PRC2 activities and enrolls PRC1 complex to further silence the chromatin through depositing monoubiquitylation of lysine 119 on H2A. Mutations in PcG genes display diverse developmental defects during shoot apical meristem (SAM) maintenance and differentiation, seed development and germi

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13

Vann, Kendra R., and Tatiana G. Kutateladze. "Architecture of PRC2 Holo Complexes." Trends in Biochemical Sciences 43, no. 7 (2018): 487–89. http://dx.doi.org/10.1016/j.tibs.2018.04.009.

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14

Takano, Junichiro, Yaeko Nakajima-Takagi, Shinsuke Ito, Haruhiko Koseki, Atsushi Iwama, and Tomokatsu Ikawa. "Variant Pcgf-PRC1 Regulates Susceptibility of PRC2 Mediated H3K27me3 to Safeguard B Cell Fate of Hematopoietic Stem/Progenitor Cells." Blood 134, Supplement_1 (2019): 3717. http://dx.doi.org/10.1182/blood-2019-129518.

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Polycomb repressive complex (PRC) resides in two major complexes PRC1 and PRC2. They cooperate with each other to coordinate proper developmental process by silencing target genes; PRC1 posits H2AK119ub1 and PRC2 catalyzes trimethylation of H3K27 (H3K27me3). The PRC1 component BMI1/PCGF4 has long been recognized to be essential in the maintenance of normal and malignant hematopoietic stem cells (HSCs). Recently, diversity of PRC1 has been noticed and PRC1 is now classified into six alternative complexes depending on PCGF proteins. In embolic stem cells, PRC1 which contains PCGF1 (PCGF1-PRC1) h

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15

Kaito, Satoshi, and Atsushi Iwama. "Pathogenic Impacts of Dysregulated Polycomb Repressive Complex Function in Hematological Malignancies." International Journal of Molecular Sciences 22, no. 1 (2020): 74. http://dx.doi.org/10.3390/ijms22010074.

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Polycomb repressive complexes (PRCs) are epigenetic regulators that mediate repressive histone modifications. PRCs play a pivotal role in the maintenance of hematopoietic stem cells through repression of target genes involved in cell proliferation and differentiation. Next-generation sequencing technologies have revealed that various hematologic malignancies harbor mutations in PRC2 genes, such as EZH2, EED, and SUZ12, and PRC1.1 genes, such as BCOR and BCORL1. Except for the activating EZH2 mutations detected in lymphoma, most of these mutations compromise PRC function and are frequently asso

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16

Hernández-Muñoz, Inmaculada, Panthea Taghavi, Coenraad Kuijl, Jacques Neefjes, and Maarten van Lohuizen. "Association of BMI1 with Polycomb Bodies Is Dynamic and Requires PRC2/EZH2 and the Maintenance DNA Methyltransferase DNMT1." Molecular and Cellular Biology 25, no. 24 (2005): 11047–58. http://dx.doi.org/10.1128/mcb.25.24.11047-11058.2005.

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ABSTRACT Polycomb group (PcG) proteins are epigenetic chromatin modifiers involved in heritable gene repression. Two main PcG complexes have been characterized. Polycomb repressive complex 2 (PRC2) is thought to be involved in the initiation of gene silencing, whereas Polycomb repressive complex 1 (PRC1) is implicated in the stable maintenance of gene repression. Here, we investigate the kinetic properties of the binding of one of the PRC1 core components, BMI1, with PcG bodies. PcG bodies are unique nuclear structures located on regions of pericentric heterochromatin, found to be the site of

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17

Fedorova, Elena M., and Alexander V. Rodionov. "TOWARDS UNDERSTANDING THE MECHANISMS OF EPIGENETIC REGULATION: PART 1. AN EVOLUTIONAL INSIGHT INTO PCG-MEDIATED GENE REPRESSION." Ecological genetics 6, no. 1 (2008): 12–19. http://dx.doi.org/10.17816/ecogen6112-19.

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The evolutionary conserved PcG proteins maintain stable transcriptional epigenetic repression, established earlier by transiently acting regulator proteins. The exact mechanism of PcG-mediated repression is not identified yet, and here we outline existing models of the repression mechanism. We also shortly summarize the current knowledge about PcG proteins and their role in various processes and present an insight into the evolution of PRC1 and PRC2 complexes.

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18

Geng, Zhuangzhuang, and Zhonghua Gao. "Mammalian PRC1 Complexes: Compositional Complexity and Diverse Molecular Mechanisms." International Journal of Molecular Sciences 21, no. 22 (2020): 8594. http://dx.doi.org/10.3390/ijms21228594.

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Polycomb group (PcG) proteins function as vital epigenetic regulators in various biological processes, including pluripotency, development, and carcinogenesis. PcG proteins form multicomponent complexes, and two major types of protein complexes have been identified in mammals to date, Polycomb Repressive Complexes 1 and 2 (PRC1 and PRC2). The PRC1 complexes are composed in a hierarchical manner in which the catalytic core, RING1A/B, exclusively interacts with one of six Polycomb group RING finger (PCGF) proteins. This association with specific PCGF proteins allows for PRC1 to be subdivided int

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Kamei, Masayuki, Abigail J. Ameri, Aileen R. Ferraro, et al. "IMITATION SWITCH is required for normal chromatin structure and gene repression in PRC2 target domains." Proceedings of the National Academy of Sciences 118, no. 4 (2021): e2010003118. http://dx.doi.org/10.1073/pnas.2010003118.

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Polycomb Group (PcG) proteins are part of an epigenetic cell memory system that plays essential roles in multicellular development, stem cell biology, X chromosome inactivation, and cancer. In animals, plants, and many fungi, Polycomb Repressive Complex 2 (PRC2) catalyzes trimethylation of histone H3 lysine 27 (H3K27me3) to assemble transcriptionally repressed facultative heterochromatin. PRC2 is structurally and functionally conserved in the model fungus Neurospora crassa, and recent work in this organism has generated insights into PRC2 control and function. To identify components of the fac

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Derkacheva, Maria, Yvonne Steinbach, Thomas Wildhaber, et al. "Arabidopsis MSI1 connects LHP1 to PRC2 complexes." EMBO Journal 32, no. 14 (2013): 2073–85. http://dx.doi.org/10.1038/emboj.2013.145.

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21

Pasini, Diego, Adrian P. Bracken, Jacob B. Hansen, Manuela Capillo, and Kristian Helin. "The Polycomb Group Protein Suz12 Is Required for Embryonic Stem Cell Differentiation." Molecular and Cellular Biology 27, no. 10 (2007): 3769–79. http://dx.doi.org/10.1128/mcb.01432-06.

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ABSTRACT Polycomb group (PcG) proteins form multiprotein complexes, called Polycomb repressive complexes (PRCs). PRC2 contains the PcG proteins EZH2, SUZ12, and EED and represses transcription through methylation of lysine (K) 27 of histone H3 (H3). Suz12 is essential for PRC2 activity and its inactivation results in early lethality of mouse embryos. Here, we demonstrate that Suz12 −/− mouse embryonic stem (ES) cells can be established and expanded in tissue culture. The Suz12 −/− ES cells are characterized by global loss of H3K27 trimethylation (H3K27me3) and higher expression levels of diffe

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Fiskus, Warren, Rekha Rao, Ramesh Balusu, et al. "Efficacy of Combined Epigenetic Targeting of Histone Methyltransferase EZH2 and Histone deacetylases Against Human Mantle Cell Lymphoma Cells." Blood 116, no. 21 (2010): 2488. http://dx.doi.org/10.1182/blood.v116.21.2488.2488.

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Abstract Abstract 2488 Lysine specific histone methylation and deacetylation are chromatin modifications that, along with DNA methylation, are involved in the epigenetic silencing of tumor suppressor genes (TSGs). This silencing is mediated by multi-protein complexes PRC (polycomb repressive complexes) 1 and 2. Of the three core protein components of PRC2, i.e., EZH2, SUZ12 and EED, EZH2 has the SET domain with its intrinsic histone methyltransferase activity, which induces the trimethylation (Me3) of lysine (K) 27 on histone (H) 3-a repressive histone modification mediating gene repression. T

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Boulay, Gaylor, Claire Rosnoblet, Cateline Guérardel, Pierre-Olivier Angrand, and Dominique Leprince. "Functional characterization of human Polycomb-like 3 isoforms identifies them as components of distinct EZH2 protein complexes." Biochemical Journal 434, no. 2 (2011): 333–42. http://dx.doi.org/10.1042/bj20100944.

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PcG (Polycomb group) proteins are conserved transcriptional repressors essential to regulate cell fate and to maintain epigenetic cellular memory. They work in concert through two main families of chromatin-modifying complexes, PRC1 (Polycomb repressive complex 1) and PRC2–4. In Drosophila, PRC2 contains the H3K27 histone methyltransferase E(Z) whose trimethylation activity towards PcG target genes is stimulated by PCL (Polycomb-like). In the present study, we have examined hPCL3, one of its three human paralogues. Through alternative splicing, hPCL3 encodes a long isoform, hPCL3L, containing

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Tavares, Lígia, Emilia Dimitrova, David Oxley, et al. "RYBP-PRC1 Complexes Mediate H2A Ubiquitylation at Polycomb Target Sites Independently of PRC2 and H3K27me3." Cell 149, no. 7 (2012): 1647–48. http://dx.doi.org/10.1016/j.cell.2012.06.011.

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Tavares, Lígia, Emilia Dimitrova, David Oxley, et al. "RYBP-PRC1 Complexes Mediate H2A Ubiquitylation at Polycomb Target Sites Independently of PRC2 and H3K27me3." Cell 148, no. 4 (2012): 664–78. http://dx.doi.org/10.1016/j.cell.2011.12.029.

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Piunti, Andrea, Edwin R. Smith, Marc A. J. Morgan, et al. "CATACOMB: An endogenous inducible gene that antagonizes H3K27 methylation activity of Polycomb repressive complex 2 via an H3K27M-like mechanism." Science Advances 5, no. 7 (2019): eaax2887. http://dx.doi.org/10.1126/sciadv.aax2887.

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Using biochemical characterization of fusion proteins associated with endometrial stromal sarcoma, we identified JAZF1 as a new subunit of the NuA4 acetyltransferase complex and CXORF67 as a subunit of the Polycomb Repressive Complex 2 (PRC2). Since CXORF67’s interaction with PRC2 leads to decreased PRC2-dependent H3K27me2/3 deposition, we propose a new name for this gene:CATACOMB(catalytic antagonist of Polycomb; official gene name:EZHIP). We mapCATACOMB’sinhibitory function to a short highly conserved region and identify a single methionine residue essential for diminution of H3K27me2/3 leve

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Cerase, Andrea, and Gian Gaetano Tartaglia. "Long non-coding RNA-polycomb intimate rendezvous." Open Biology 10, no. 9 (2020): 200126. http://dx.doi.org/10.1098/rsob.200126.

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The interaction between polycomb-repressive complexes 1/2 (PRC1/2) and long non-coding RNA (lncRNA), such as the X inactive specific transcript Xist and the HOX transcript antisense RNA (HOTAIR), has been the subject of intense debate. While cross-linking, immuno-precipitation and super-resolution microscopy argue against direct interaction of Polycomb with some lncRNAs, there is increasing evidence supporting the ability of both PRC1 and PRC2 to functionally associate with RNA. Recent data indicate that these interactions are in most cases spurious, but nonetheless crucial for a number of cel

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Sunwoo, Hongjae, John Y. Wu, and Jeannie T. Lee. "The Xist RNA-PRC2 complex at 20-nm resolution reveals a low Xist stoichiometry and suggests a hit-and-run mechanism in mouse cells." Proceedings of the National Academy of Sciences 112, no. 31 (2015): E4216—E4225. http://dx.doi.org/10.1073/pnas.1503690112.

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X-chromosome inactivation (XCI) is initiated by the long noncoding RNA Xist, which coats the inactive X (Xi) and targets Polycomb repressive complex 2 (PRC2) in cis. Epigenomic analyses have provided significant insight into Xist binding patterns and chromatin organization of the Xi. However, such epigenomic analyses are limited by averaging of population-wide dynamics and do not inform behavior of single cells. Here we view Xist RNA and the Xi at 20-nm resolution using STochastic Optical Reconstruction Microscopy (STORM) in mouse cells. We observe dynamics at the single-cell level not predict

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Xu, Jian, Zhen Shao, Dan Li, et al. "Developmental Control of Polycomb Subunit Composition Mediates a Switch to Non-Canonical Functions during Hematopoiesis." Blood 124, no. 21 (2014): 241. http://dx.doi.org/10.1182/blood.v124.21.241.241.

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Abstract The epigenetic machinery plays crucial roles in hematopoiesis, and its deregulation drives the pathogenesis of blood disorders. Polycomb Repressive Complex 2 (PRC2) is a major class of epigenetic repressor that catalyzes the di/tri-methylation of histone H3 lysine 27 (or H3K27me2/3). The canonical PRC2 complex consists of EED, SUZ12, and the histone methyltransferase EZH2. The functions of PRC2 in hematopoiesis remain elusive due in large to the existence of two highly related enzymatic subunits EZH1 and EZH2. While amplification or overexpression of PRC2 proteins is common in many ca

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Oliva, Moran, Yana Butenko, Tzung-Fu Hsieh, et al. "FIE, a nuclear PRC2 protein, forms cytoplasmic complexes inArabidopsis thaliana." Journal of Experimental Botany 67, no. 21 (2016): 6111–23. http://dx.doi.org/10.1093/jxb/erw373.

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Sarma, Kavitha, Raphael Margueron, Alexey Ivanov, Vincenzo Pirrotta, and Danny Reinberg. "Ezh2 Requires PHF1 To Efficiently Catalyze H3 Lysine 27 Trimethylation In Vivo." Molecular and Cellular Biology 28, no. 8 (2008): 2718–31. http://dx.doi.org/10.1128/mcb.02017-07.

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ABSTRACT The mammalian Polycomblike protein PHF1 was previously shown to interact with the Polycomb group (PcG) protein Ezh2, a histone methyltransferase whose activity is pivotal in sustaining gene repression during development and in adulthood. As Ezh2 is active only when part of the Polycomb Repressive Complexes (PRC2-PRC4), we examined the functional role of its interaction with PHF1. Chromatin immunoprecipitation experiments revealed that PHF1 resides along with Ezh2 at Ezh2-regulated genes such as the HoxA loci and the non-Hox MYT1 and WNT1 genes. Knockdown of PHF1 or of Ezh2 led to up-r

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Kadoch, Cigall, Robert A. Copeland, and Heike Keilhack. "PRC2 and SWI/SNF Chromatin Remodeling Complexes in Health and Disease." Biochemistry 55, no. 11 (2016): 1600–1614. http://dx.doi.org/10.1021/acs.biochem.5b01191.

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Moody, James D., Shiri Levy, Julie Mathieu, et al. "First critical repressive H3K27me3 marks in embryonic stem cells identified using designed protein inhibitor." Proceedings of the National Academy of Sciences 114, no. 38 (2017): 10125–30. http://dx.doi.org/10.1073/pnas.1706907114.

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The polycomb repressive complex 2 (PRC2) histone methyltransferase plays a central role in epigenetic regulation in development and in cancer, and hence to interrogate its role in a specific developmental transition, methods are needed for disrupting function of the complex with high temporal and spatial precision. The catalytic and substrate recognition functions of PRC2 are coupled by binding of the N-terminal helix of the Ezh2 methylase to an extended groove on the EED trimethyl lysine binding subunit. Disrupting PRC2 function can in principle be achieved by blocking this single interaction

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Bakhshinyan, David, Ashley A. Adile, Chitra Venugopal, and Sheila K. Singh. "Bmi1 – A Path to Targeting Cancer Stem Cells." European Oncology & Haematology 13, no. 02 (2017): 147. http://dx.doi.org/10.17925/eoh.2017.13.02.147.

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The Polycomb group (PcG) genes encode for proteins comprising two multiprotein complexes, Polycomb repressive complex 1 (PRC1) and Polycomb repressive complex 2 (PRC2). Although the initial discovery of PcG genes was made in Drosophila, as transcriptional repressors of homeotic (HOX) genes. Polycomb repressive complexes have been since implicated in regulating a wide range of cellular processes, including differentiation and self-renewal in normal and cancer stem cells. Bmi1, a subunit of PRC1, has been long implicated in driving self-renewal, the key property of stem cells. Subsequent studies

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Stojic, Lovorka, Zuzana Jasencakova, Carolina Prezioso, et al. "Chromatin regulated interchange between polycomb repressive complex 2 (PRC2)-Ezh2 and PRC2-Ezh1 complexes controls myogenin activation in skeletal muscle cells." Epigenetics & Chromatin 4, no. 1 (2011): 16. http://dx.doi.org/10.1186/1756-8935-4-16.

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Panditharatna, Eshini, Neekesh Dharia, Deyao Li, et al. "EXTH-37. TARGETING EPIGENETIC VULNERABILITIES IDENTIFIED FROM A CRISPR SCREEN IN H3.3K27M DIPG." Neuro-Oncology 22, Supplement_2 (2020): ii95. http://dx.doi.org/10.1093/neuonc/noaa215.391.

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Abstract Children diagnosed with diffuse intrinsic pontine glioma (DIPG), a type of high grade glioma in the brainstem, currently have a dismal 5-year overall survival of only 2%. The majority of DIPG patients harbor a K27M mutation in histone 3.3 encoding genes (H3.3K27M). To understand if the aberrant epigenetic landscape induced by H3.3K27M provides an opportunity for novel targeted therapies, we conducted the first CRISPR/Cas9 screen using a focused library of 1,350 epigenetic regulatory and cancer related genes in six H3.3K27M DIPG patient-derived primary neurosphere cell lines. We identi

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Basenko, Evelina Y., Takahiko Sasaki, Lexiang Ji, et al. "Genome-wide redistribution of H3K27me3 is linked to genotoxic stress and defective growth." Proceedings of the National Academy of Sciences 112, no. 46 (2015): E6339—E6348. http://dx.doi.org/10.1073/pnas.1511377112.

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H3K9 methylation directs heterochromatin formation by recruiting multiple heterochromatin protein 1 (HP1)-containing complexes that deacetylate histones and methylate cytosine bases in DNA. In Neurospora crassa, a single H3K9 methyltransferase complex, called the DIM-5,-7,-9, CUL4, DDB1 Complex (DCDC), is required for normal growth and development. DCDC-deficient mutants are hypersensitive to the genotoxic agent methyl methanesulfonate (MMS), but the molecular basis of genotoxic stress is unclear. We found that both the MMS sensitivity and growth phenotypes of DCDC-deficient strains are suppre

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Huang, Yu-Chang, Hitomi Hasegawa, Shin-Wei Wang, et al. "Jun Dimerization Protein 2 Controls Senescence and Differentiation via Regulating Histone Modification." Journal of Biomedicine and Biotechnology 2011 (2011): 1–13. http://dx.doi.org/10.1155/2011/569034.

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Transcription factor, Jun dimerization protein 2 (JDP2), binds directly to histones and DNAs and then inhibits the p300-mediated acetylation both of core histones and of reconstituted nucleosomes that contain JDP2 recognition DNA sequences. JDP2 plays a key role as a repressor of adipocyte differentiation by regulation of the expression of the gene C/EBPδ via inhibition of histone acetylation. Moreover, JDP2-deficient mouse embryonic fibroblasts (JDP2−/−MEFs) are resistant to replicative senescence. JDP2 inhibits the recruitment of polycomb repressive complexes (PRC1 and PRC2) to the promoter

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Du, Junqing, Brian Kirk, Jia Zeng, Jianpeng Ma, and Qinghua Wang. "Three classes of response elements for human PRC2 and MLL1/2–Trithorax complexes." Nucleic Acids Research 46, no. 17 (2018): 8848–64. http://dx.doi.org/10.1093/nar/gky595.

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Godovikova, Valentina, M. Paula Goetting-Minesky, and J. Christopher Fenno. "Composition and Localization of Treponema denticola Outer Membrane Complexes." Infection and Immunity 79, no. 12 (2011): 4868–75. http://dx.doi.org/10.1128/iai.05701-11.

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ABSTRACTTheTreponema denticolaouter membrane lipoprotein-protease complex (dentilisin) contributes to periodontal disease by degrading extracellular matrix components and disrupting intercellular host signaling pathways. We recently demonstrated thatprcB, located upstream of and cotranscribed withprcAandprtP, encodes a 22-kDa lipoprotein that interacts with PrtP and is required for its activity. Here we further characterize products of the protease locus and their roles in expression, formation, and localization of outer membrane complexes. PrcB migrates in native gels as part of a >400-kDa

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Tanaka, Tomoyuki, Yaeko Nakajima-Takagi, Sha Si, et al. "Role of the Polycomb Gene Bcor in Hematopoiesis." Blood 124, no. 21 (2014): 4312. http://dx.doi.org/10.1182/blood.v124.21.4312.4312.

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Abstract Polycomb group (PcG) proteins are epigenetic regulators crucial for the maintenance and differentiation of stem cells. PcG proteins form in the nucleus two kinds of complexes, PRC (polycomb repressive complex) 1 containing Pcgf family proteins and PRC2. PRC1 ubiquitylates histone H2A at lysine 119 and PRC2 trimethylates lysine 27 of histone H3. Bcor (BCL6 corepressor) together with Pcgf1 has recently been demonstrated to form a non-canonical PRC1 distinct from canonical PRC1 containing Cbx and Bmi1/Pcgf4. Of note, recurrent somatic mutations have been identified in BCOR in myeloid mal

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Tie, Feng, Carl A. Stratton, Rebeccah L. Kurzhals, and Peter J. Harte. "The N Terminus of Drosophila ESC Binds Directly to Histone H3 and Is Required for E(Z)-Dependent Trimethylation of H3 Lysine 27." Molecular and Cellular Biology 27, no. 6 (2007): 2014–26. http://dx.doi.org/10.1128/mcb.01822-06.

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ABSTRACT Polycomb group proteins mediate heritable transcriptional silencing and function through multiprotein complexes that methylate and ubiquitinate histones. The 600-kDa E(Z)/ESC complex, also known as Polycomb repressive complex 2 (PRC2), specifically methylates histone H3 lysine 27 (H3 K27) through the intrinsic histone methyltransferase (HMTase) activity of the E(Z) SET domain. By itself, E(Z) exhibits no detectable HMTase activity and requires ESC for methylation of H3 K27. The molecular basis for this requirement is unknown. ESC binds directly, via its C-terminal WD repeats (β-propel

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Giaimo, Benedetto Daniele, Teresa Robert-Finestra, Franz Oswald, Joost Gribnau, and Tilman Borggrefe. "Chromatin Regulator SPEN/SHARP in X Inactivation and Disease." Cancers 13, no. 7 (2021): 1665. http://dx.doi.org/10.3390/cancers13071665.

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Enzymes, such as histone methyltransferases and demethylases, histone acetyltransferases and deacetylases, and DNA methyltransferases are known as epigenetic modifiers that are often implicated in tumorigenesis and disease. One of the best-studied chromatin-based mechanism is X chromosome inactivation (XCI), a process that establishes facultative heterochromatin on only one X chromosome in females and establishes the right dosage of gene expression. The specificity factor for this process is the long non-coding RNA Xinactivespecifictranscript (Xist), which is upregulated from one X chromosome

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Yamamoto, Maiko, Yoshiaki Suwa, Kohta Sugiyama, et al. "The PRDM14–CtBP1/2–PRC2 complex regulates transcriptional repression during the transition from primed to naïve pluripotency." Journal of Cell Science 133, no. 15 (2020): jcs240176. http://dx.doi.org/10.1242/jcs.240176.

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ABSTRACTThe pluripotency-associated transcriptional network is regulated by a core circuitry of transcription factors. The PR domain-containing protein PRDM14 maintains pluripotency by activating and repressing transcription in a target gene-dependent manner. However, the mechanisms underlying dichotomic switching of PRDM14-mediated transcriptional control remain elusive. Here, we identified C-terminal binding protein 1 and 2 (CtBP1 and CtBP2; generically referred to as CtBP1/2) as components of the PRDM14-mediated repressive complex. CtBP1/2 binding to PRDM14 depends on CBFA2T2, a core compon

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Tyagi, Mudit, Sonia Zicari, Kalamo Farley, Lin Sun, and Gary Simon. "P-A1 CBF-1 promotes the establishment and maintenance of HIV latency by recruiting Polycomb repressive complexes, PRC1 and PRC2, at HIV LTR." JAIDS Journal of Acquired Immune Deficiency Syndromes 77 (April 2018): 53. http://dx.doi.org/10.1097/01.qai.0000532644.93546.51.

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Schubert, Daniel. "Evolution of Polycomb-group function in the green lineage." F1000Research 8 (March 8, 2019): 268. http://dx.doi.org/10.12688/f1000research.16986.1.

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Epigenetic gene regulation ensures the mitotically or meiotically stable heritability (or both) of gene expression or protein activity states and maintains repetitive element repression and cellular identities. The repressive Polycomb-group (PcG) proteins consist of several large complexes that control cellular memory by acting on chromatin and are antagonized by the Trithorax-group proteins. Especially, Polycomb repressive complex 2 (PRC2) is highly conserved in plants and animals but its function in unicellular eukaryotes and during land plant evolution is less understood. Additional PcG com

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Nakamura, Shunsuke, and Atsushi Iwama. "Bmi1 Confers Stress Resistance to Self-Renewing Hematopoietic Stem Cells." Blood 116, no. 21 (2010): 1607. http://dx.doi.org/10.1182/blood.v116.21.1607.1607.

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Abstract Abstract 1607 The polycomb group (PcG) proteins form chromatin-modifying complexes that implement transcriptional silencing. There are two major PcG complexes, polycomb repressive complex (PRC) 1 and PRC2. PRC1 ubiquitylates histone H2A at lysine 119 and PRC2 trimethylates lysine 27 of histone H3. Among PcG proteins, Bmi1, a core component of PRC1, plays an essential role in the self-renewal and maintenance of various kinds of stem cells including hematopoietic stem cells (HSCs), neural stem cells, and leukemic stem cells. We previously reported that forced expression of Bmi1 using a

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Zhou, Yue, Emmanuel Tergemina, Haitao Cui, et al. "Ctf4-related protein recruits LHP1-PRC2 to maintain H3K27me3 levels in dividing cells in Arabidopsis thaliana." Proceedings of the National Academy of Sciences 114, no. 18 (2017): 4833–38. http://dx.doi.org/10.1073/pnas.1620955114.

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Polycomb Repressive Complex (PRC) 2 catalyzes the H3K27me3 modification that warrants inheritance of a repressive chromatin structure during cell division, thereby assuring stable target gene repression in differentiated cells. It is still under investigation how H3K27me3 is passed on from maternal to filial strands during DNA replication; however, cell division can reinforce H3K27me3 coverage at target regions. To identify novel factors involved in the Polycomb pathway in plants, we performed a forward genetic screen for enhancers of the like heterochromatin protein 1 (lhp1) mutant, which sho

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Shinoda, Daisuke, Yaeko Nakajima-Takagi, Motohiko Oshima, et al. "Insufficiency of Non-Canonical PRC1 Complex Cooperates with an Activating JAK2 Mutation in the Pathogenesis of Myelofibrosis." Blood 132, Supplement 1 (2018): 100. http://dx.doi.org/10.1182/blood-2018-99-117741.

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Abstract Introduction: PcG proteins form two main multiprotein complexes, Polycomb repressive complex 1 (PRC1) and PRC2. They repress the transcription of target genes. Polycomb group ring finger protein1 (PCGF1) is a component of PRC1.1, a non-canonical PRC1.1 that monoubiquitylates H2A at lysine 119 in a manner independent of H3K27me3. Several groups including ours showed that the loss of Ezh2, a component of PRC2, promotes the development of JAK2 V617F-induced Myelofibrosis (MF) in mice. However, the role of PRC1.1 in hematologic malignancies is still not fully understood. We found that the

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Kia, Sima Kheradmand, Marcin M. Gorski, Stavros Giannakopoulos, and C. Peter Verrijzer. "SWI/SNF Mediates Polycomb Eviction and Epigenetic Reprogramming of the INK4b-ARF-INK4a Locus." Molecular and Cellular Biology 28, no. 10 (2008): 3457–64. http://dx.doi.org/10.1128/mcb.02019-07.

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ABSTRACT Stable silencing of the INK4b-ARF-INK4a tumor suppressor locus occurs in a variety of human cancers, including malignant rhabdoid tumors (MRTs). MRTs are extremely aggressive cancers caused by the loss of the hSNF5 subunit of the SWI/SNF chromatin-remodeling complex. We found previously that, in MRT cells, hSNF5 is required for p16 INK4a induction, mitotic checkpoint activation, and cellular senescence. Here, we investigated how the balance between Polycomb group (PcG) silencing and SWI/SNF activation affects epigenetic control of the INK4b-ARF-INK4a locus in MRT cells. hSNF5 reexpres

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