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Journal articles on the topic 'Polycomb complex'

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Published: 31 August 2024

Last updated: 31 July 2025

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1

Strutt, H., and R. Paro. "The polycomb group protein complex of Drosophila melanogaster has different compositions at different target genes." Molecular and Cellular Biology 17, no. 12 (1997): 6773–83. http://dx.doi.org/10.1128/mcb.17.12.6773.

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In Drosophila the Polycomb group genes are required for the long-term maintenance of the repressed state of many developmental regulatory genes. Their gene products are thought to function in a common multimeric complex that associates with Polycomb group response elements (PREs) in target genes and regulates higher-order chromatin structure. We show that the chromodomain of Polycomb is necessary for protein-protein interactions within a Polycomb-Polyhomeotic complex. In addition, Posterior Sex Combs protein coimmunoprecipitates Polycomb and Polyhomeotic, indicating that they are members of a

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2

Chiang, A., M. B. O'Connor, R. Paro, J. Simon, and W. Bender. "Discrete Polycomb-binding sites in each parasegmental domain of the bithorax complex." Development 121, no. 6 (1995): 1681–89. http://dx.doi.org/10.1242/dev.121.6.1681.

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The Polycomb protein of Drosophila melanogaster maintains the segmental expression limits of the homeotic genes in the bithorax complex. Polycomb-binding sites within the bithorax complex were mapped by immunostaining of salivary gland polytene chromosomes. Polycomb bound to four DNA fragments, one in each of four successive parasegmental regulatory regions. These fragments correspond exactly to the ones that can maintain segmentally limited expression of a lacZ reporter gene. Thus, Polycomb acts directly on discrete multiple sites in bithorax regulatory DNA. Constructs combining fragments fro

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3

De, Sandip, Natalie D. Gehred, Miki Fujioka, Fountane W. Chan, James B. Jaynes, and Judith A. Kassis. "Defining the Boundaries of Polycomb Domains in Drosophila." Genetics 216, no. 3 (2020): 689–700. http://dx.doi.org/10.1534/genetics.120.303642.

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Polycomb group (PcG) proteins are an important group of transcriptional repressors that act by modifying chromatin. PcG target genes are covered by the repressive chromatin mark H3K27me3. Polycomb repressive complex 2 (PRC2) is a multiprotein complex that is responsible for generating H3K27me3. In Drosophila, PRC2 is recruited by Polycomb Response Elements (PREs) and then trimethylates flanking nucleosomes, spreading the H3K27me3 mark over large regions of the genome, the “Polycomb domains.” What defines the boundary of a Polycomb domain? There is experimental evidence that insulators, PolII,

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4

Ali, Janann Y., and Welcome Bender. "Cross-Regulation among the Polycomb Group Genes in Drosophila melanogaster." Molecular and Cellular Biology 24, no. 17 (2004): 7737–47. http://dx.doi.org/10.1128/mcb.24.17.7737-7747.2004.

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ABSTRACT Genes of the Polycomb group in Drosophila melanogaster function as long-term transcriptional repressors. A few members of the group encode proteins found in two evolutionarily conserved chromatin complexes, Polycomb repressive complex 1 (PRC1) and the ESC-E(Z) complex. The majority of the group, lacking clear biochemical functions, might be indirect regulators. The transcript levels of seven Polycomb group genes were assayed in embryos mutant for various other genes in the family. Three Polycomb group genes were identified as upstream positive regulators of the core components of PRC1

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5

Seong, Ihn Sik, Juliana M. Woda, Ji-Joon Song, et al. "Huntingtin facilitates polycomb repressive complex 2." Human Molecular Genetics 19, no. 4 (2009): 573–83. http://dx.doi.org/10.1093/hmg/ddp524.

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6

Mohd-Sarip, Adone, Jan A. van der Knaap, Claire Wyman, Roland Kanaar, Paul Schedl, and C. Peter Verrijzer. "Architecture of a Polycomb Nucleoprotein Complex." Molecular Cell 24, no. 1 (2006): 91–100. http://dx.doi.org/10.1016/j.molcel.2006.08.007.

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7

Iragavarapu, Akhil Gargey, Liqi Yao, and Vignesh Kasinath. "Structural insights into the interactions of Polycomb Repressive Complex 2 with chromatin." Biochemical Society Transactions 49, no. 6 (2021): 2639–53. http://dx.doi.org/10.1042/bst20210450.

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Polycomb repressive complexes are a family of chromatin modifier enzymes which are critical for regulating gene expression and maintaining cell-type identity. The reversible chemical modifications of histone H3 and H2A by the Polycomb proteins are central to its ability to function as a gene silencer. PRC2 is both a reader and writer of the tri-methylation of histone H3 lysine 27 (H3K27me3) which serves as a marker for transcription repression, and heterochromatin boundaries. Over the last few years, several studies have provided key insights into the mechanisms regulating the recruitment and

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8

Iwata, Shintaro, Hisanori Takenobu, Hajime Kageyama, et al. "Polycomb group molecule PHC3 regulates polycomb complex composition and prognosis of osteosarcoma." Cancer Science 101, no. 7 (2010): 1646–52. http://dx.doi.org/10.1111/j.1349-7006.2010.01586.x.

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9

Lo, Stanley M., Nitin K. Ahuja, and Nicole J. Francis. "Polycomb Group Protein Suppressor 2 of Zeste Is a Functional Homolog of Posterior Sex Combs." Molecular and Cellular Biology 29, no. 2 (2008): 515–25. http://dx.doi.org/10.1128/mcb.01044-08.

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ABSTRACT The Drosophila melanogaster Polycomb group protein Posterior Sex Combs is a component of Polycomb repressive complex 1 and is central to Polycomb group-mediated silencing. A related Polycomb group gene, Suppressor 2 of zeste, is thought to be partially redundant in function. The two proteins share a small region of homology but also contain regions of unconserved sequences. Here we report a biochemical characterization of Suppressor 2 of zeste. Like Posterior Sex Combs, Suppressor 2 of zeste binds DNA, compacts chromatin, and inhibits chromatin remodeling. Interestingly, the regions o

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10

LaJeunesse, D., and A. Shearn. "E(z): a polycomb group gene or a trithorax group gene?" Development 122, no. 7 (1996): 2189–97. http://dx.doi.org/10.1242/dev.122.7.2189.

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The products of the Polycomb group of genes are cooperatively involved in repressing expression of homeotic selector genes outside of their appropriate anterior/posterior boundaries. Loss of maternal and/or zygotic function of Polycomb group genes results in the ectopic expression of both Antennapedia Complex and Bithorax Complex genes. The products of the trithorax group of genes are cooperatively involved in maintaining active expression of homeotic selector genes within their appropriate anterior/posterior boundaries. Loss of maternal and/or zygotic function of trithorax group genes results

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11

Lewis, Zachary A. "Polycomb Group Systems in Fungi: New Models for Understanding Polycomb Repressive Complex 2." Trends in Genetics 33, no. 3 (2017): 220–31. http://dx.doi.org/10.1016/j.tig.2017.01.006.

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12

Hu, Chi-Kuo, Wei Wang, Julie Brind’Amour, et al. "Vertebrate diapause preserves organisms long term through Polycomb complex members." Science 367, no. 6480 (2020): 870–74. http://dx.doi.org/10.1126/science.aaw2601.

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Diapause is a state of suspended development that helps organisms survive extreme environments. How diapause protects living organisms is largely unknown. Using the African turquoise killifish (Nothobranchius furzeri), we show that diapause preserves complex organisms for extremely long periods of time without trade-offs for subsequent adult growth, fertility, and life span. Transcriptome analyses indicate that diapause is an active state, with dynamic regulation of metabolism and organ development genes. The most up-regulated genes in diapause include Polycomb complex members. The chromatin m

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13

Rank, Gerhard, Matthias Prestel, and Renato Paro. "Transcription through Intergenic Chromosomal Memory Elements of the Drosophila Bithorax Complex Correlates with an Epigenetic Switch." Molecular and Cellular Biology 22, no. 22 (2002): 8026–34. http://dx.doi.org/10.1128/mcb.22.22.8026-8034.2002.

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ABSTRACT The proteins of the trithorax and Polycomb groups maintain the differential expression pattern of homeotic genes established by the early embryonic patterning system during development. These proteins generate stable and heritable chromatin structures by acting via particular chromosomal memory elements. We established a transgenic assay system showing that the Polycomb group response elements bxd and Mcp confer epigenetic inheritance throughout development. With previously published data for the Fab7 cellular memory module, we confirmed the cellular memory function of Polycomb group

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14

Torigata, Kosuke, Okuzaki Daisuke, Satomi Mukai, et al. "LATS2 Positively Regulates Polycomb Repressive Complex 2." PLOS ONE 11, no. 7 (2016): e0158562. http://dx.doi.org/10.1371/journal.pone.0158562.

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15

Barrero, Maria J., and Juan Carlos Izpisua Belmonte. "Polycomb complex recruitment in pluripotent stem cells." Nature Cell Biology 15, no. 4 (2013): 348–50. http://dx.doi.org/10.1038/ncb2723.

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16

Deckard, Charles E., and Jonathan T. Sczepanski. "Polycomb repressive complex 2 binds RNA irrespective of stereochemistry." Chemical Communications 54, no. 85 (2018): 12061–64. http://dx.doi.org/10.1039/c8cc07433j.

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17

Costa, Silvia, and Caroline Dean. "Storing memories: the distinct phases of Polycomb-mediated silencing of Arabidopsis FLC." Biochemical Society Transactions 47, no. 4 (2019): 1187–96. http://dx.doi.org/10.1042/bst20190255.

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Abstract Polycomb-mediated epigenetic silencing is central to correct growth and development in higher eukaryotes. The evolutionarily conserved Polycomb repressive complex 2 (PRC2) transcriptionally silences target genes through a mechanism requiring the histone modification H3K27me3. However, we still do not fully understand what defines Polycomb targets, how their expression state is switched from epigenetically ON to OFF and how silencing is subsequently maintained through many cell divisions. An excellent system in which to dissect the sequence of events underlying an epigenetic switch is

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18

Amiad Pavlov, Daria, CP Unnikannan, Dana Lorber, et al. "The LINC Complex Inhibits Excessive Chromatin Repression." Cells 12, no. 6 (2023): 932. http://dx.doi.org/10.3390/cells12060932.

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The Linker of Nucleoskeleton and Cytoskeleton (LINC) complex transduces nuclear mechanical inputs suggested to control chromatin organization and gene expression; however, the underlying mechanism is currently unclear. We show here that the LINC complex is needed to minimize chromatin repression in muscle tissue, where the nuclei are exposed to significant mechanical inputs during muscle contraction. To this end, the genomic binding profiles of Polycomb, Heterochromatin Protein1 (HP1a) repressors, and of RNA-Pol II were studied in Drosophila larval muscles lacking functional LINC complex. A si

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19

Gahan, James M., Fabian Rentzsch, and Christine E. Schnitzler. "The genetic basis for PRC1 complex diversity emerged early in animal evolution." Proceedings of the National Academy of Sciences 117, no. 37 (2020): 22880–89. http://dx.doi.org/10.1073/pnas.2005136117.

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Polycomb group proteins are essential regulators of developmental processes across animals. Despite their importance, studies on Polycomb are often restricted to classical model systems and, as such, little is known about the evolution of these important chromatin regulators. Here we focus on Polycomb Repressive Complex 1 (PRC1) and trace the evolution of core components of canonical and non-canonical PRC1 complexes in animals. Previous work suggested that a major expansion in the number of PRC1 complexes occurred in the vertebrate lineage. We show that the expansion of the Polycomb Group RING

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20

Muller, J., S. Gaunt, and P. A. Lawrence. "Function of the Polycomb protein is conserved in mice and flies." Development 121, no. 9 (1995): 2847–52. http://dx.doi.org/10.1242/dev.121.9.2847.

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A key aspect of determination--the acquisition and propagation of cell fates--is the initiation of patterns of selector gene expression and their maintenance in groups of cells as they divide and develop. In Drosophila, in those groups of cells where particular selector genes must remain inactive, it is the Polycomb-Group of genes that keep them silenced. Here we show that M33, a mouse homologue of the Drosophila Polycomb protein, can substitute for Polycomb in transgenic flies. Polycomb protein is thought to join with other Polycomb-Group proteins to build a complex that silences selector gen

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21

Chen, Xin, Mark Hiller, Yasemin Sancak, and Margaret T. Fuller. "Tissue-Specific TAFs Counteract Polycomb to Turn on Terminal Differentiation." Science 310, no. 5749 (2005): 869–72. http://dx.doi.org/10.1126/science.1118101.

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Polycomb transcriptional silencing machinery is implicated in the maintenance of precursor fates, but how this repression is reversed to allow cell differentiation is unknown. Here we show that testis-specific TAF (TBP-associated factor) homologs required for terminal differentiation of male germ cells may activate target gene expression in part by counteracting repression by Polycomb. Chromatin immunoprecipitation revealed that testis TAFs bind to target promoters, reduce Polycomb binding, and promote local accumulation of H3K4me3, a mark of Trithorax action. Testis TAFs also promoted relocal

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22

Semprich, Claudia I., Lindsay Davidson, Adriana Amorim Torres, et al. "ERK1/2 signalling dynamics promote neural differentiation by regulating chromatin accessibility and the polycomb repressive complex." PLOS Biology 20, no. 12 (2022): e3000221. http://dx.doi.org/10.1371/journal.pbio.3000221.

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Fibroblast growth factor (FGF) is a neural inducer in many vertebrate embryos, but how it regulates chromatin organization to coordinate the activation of neural genes is unclear. Moreover, for differentiation to progress, FGF signalling must decline. Why these signalling dynamics are required has not been determined. Here, we show that dephosphorylation of the FGF effector kinase ERK1/2 rapidly increases chromatin accessibility at neural genes in mouse embryos, and, using ATAC-seq in human embryonic stem cell derived spinal cord precursors, we demonstrate that this occurs genome-wide across n

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23

Verrijzer, C. Peter. "Goldilocks meets Polycomb." Genes & Development 36, no. 19-20 (2022): 1043–45. http://dx.doi.org/10.1101/gad.350248.122.

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The Polycomb system modulates chromatin structure to maintain gene repression during cell differentiation. Polycomb repression involves methylation of histone H3K27 (H3K27me3) by Polycomb repressive complex 2 (PRC2), monoubiquitylation of H2A (H2Aub1) by noncanonical PRC1 (ncPRC1), and chromatin compaction by canonical PRC1 (cPRC1), which is independent of its enzymatic activity. Puzzlingly, Polycomb repression also requires deubiquitylation of H2Aub1 by Polycomb repressive deubiquitinase (PR-DUB). In this issue ofGenes & Development, Bonnet and colleagues (pp. 1046–1061) resolve this para

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24

Dai, Fei‐Fei, Jing Chen, Zhen Ma та ін. "The polycomb protein complex interacts with GATA‐6/PPARα to inhibit α‐MHC expression". Development, Growth & Differentiation 67, № 1 (2024): 23–32. https://doi.org/10.1111/dgd.12953.

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AbstractTranscription factors collaborate with epigenetic regulatory factors to orchestrate cardiac differentiation for heart development, but the underlying mechanism is not fully understood. Here, we report that GATA‐6 induces cardiac differentiation but peroxisome proliferator‐activated receptor α (PPARα) reverses GATA‐6‐induced cardiac differentiation, possibly because GATA‐6/PPARα recruits the polycomb protein complex containing EZH2/Ring1b/BMI1 to the promoter of the cardiac‐specific α‐myosin heavy chain (α‐MHC) gene and suppresses α‐MHC expression, which ultimately inhibits cardiac diff

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25

Fitzgerald, Daniel P., and Welcome Bender. "Polycomb Group Repression Reduces DNA Accessibility." Molecular and Cellular Biology 21, no. 19 (2001): 6585–97. http://dx.doi.org/10.1128/mcb.21.19.6585-6597.2001.

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ABSTRACT The Polycomb group proteins are responsible for long-term repression of a number of genes in Drosophila melanogaster, including the homeotic genes of the bithorax complex. The Polycomb protein is thought to alter the chromatin structure of its target genes, but there has been little direct evidence for this model. In this study, the chromatin structure of the bithorax complex was probed with three separate assays for DNA accessibility: (i) activation of polymerase II (Pol II) transcription by Gal4, (ii) transcription by the bacteriophage T7 RNA polymerase (T7RNAP), and (iii) FLP-media

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26

AN, Yan-Rong, Jian-Bin XU, and Hai-Long AN. "Polycomb group protein complex involved in plant vernalization." Hereditas (Beijing) 33, no. 3 (2011): 207–12. http://dx.doi.org/10.3724/sp.j.1005.2011.00207.

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27

Davidovich, Chen, Leon Zheng, Karen J. Goodrich, and Thomas R. Cech. "Promiscuous RNA binding by Polycomb repressive complex 2." Nature Structural & Molecular Biology 20, no. 11 (2013): 1250–57. http://dx.doi.org/10.1038/nsmb.2679.

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28

Francis, N. J. "Chromatin Compaction by a Polycomb Group Protein Complex." Science 306, no. 5701 (2004): 1574–77. http://dx.doi.org/10.1126/science.1100576.

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29

Francis, Nicole J., Andrew J. Saurin, Zhaohui Shao, and Robert E. Kingston. "Reconstitution of a Functional Core Polycomb Repressive Complex." Molecular Cell 8, no. 3 (2001): 545–56. http://dx.doi.org/10.1016/s1097-2765(01)00316-1.

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30

Bratkowski, Matthew, Xin Yang, and Xin Liu. "Polycomb repressive complex 2 in an autoinhibited state." Journal of Biological Chemistry 292, no. 32 (2017): 13323–32. http://dx.doi.org/10.1074/jbc.m117.787572.

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31

Danishuddin, Naidu Subbarao, Mohammad Faheem, and Shahper Nazeer Khan. "Polycomb repressive complex 2 inhibitors: emerging epigenetic modulators." Drug Discovery Today 24, no. 1 (2019): 179–88. http://dx.doi.org/10.1016/j.drudis.2018.07.002.

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32

Kouznetsova, Valentina L., Alex Tchekanov, Xiaoming Li, Xiaowen Yan, and Igor F. Tsigelny. "Polycomb repressive 2 complex—Molecular mechanisms of function." Protein Science 28, no. 8 (2019): 1387–99. http://dx.doi.org/10.1002/pro.3647.

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33

Naxerova, Kamila. "A new function for polycomb in immune evasion." Science Translational Medicine 11, no. 514 (2019): eaaz3718. http://dx.doi.org/10.1126/scitranslmed.aaz3718.

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34

Flora, Pooja, Gil Dalal, Idan Cohen, and Elena Ezhkova. "Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells." Genes 12, no. 10 (2021): 1485. http://dx.doi.org/10.3390/genes12101485.

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Populations of resident stem cells (SCs) are responsible for maintaining, repairing, and regenerating adult tissues. In addition to having the capacity to generate all the differentiated cell types of the tissue, adult SCs undergo long periods of quiescence within the niche to maintain themselves. The process of SC renewal and differentiation is tightly regulated for proper tissue regeneration throughout an organisms’ lifetime. Epigenetic regulators, such as the polycomb group (PcG) of proteins have been implicated in modulating gene expression in adult SCs to maintain homeostatic and regenera

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35

Kanhere, Aditi, Keijo Viiri, Carla C. Araújo, et al. "Short RNAs Are Transcribed from Repressed Polycomb Target Genes and Interact with Polycomb Repressive Complex-2." Molecular Cell 38, no. 5 (2010): 675–88. http://dx.doi.org/10.1016/j.molcel.2010.03.019.

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36

Vijayanathan, Mallika, María Guadalupe Trejo-Arellano, and Iva Mozgová. "Polycomb Repressive Complex 2 in Eukaryotes—An Evolutionary Perspective." Epigenomes 6, no. 1 (2022): 3. http://dx.doi.org/10.3390/epigenomes6010003.

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Polycomb repressive complex 2 (PRC2) represents a group of evolutionarily conserved multi-subunit complexes that repress gene transcription by introducing trimethylation of lysine 27 on histone 3 (H3K27me3). PRC2 activity is of key importance for cell identity specification and developmental phase transitions in animals and plants. The composition, biochemistry, and developmental function of PRC2 in animal and flowering plant model species are relatively well described. Recent evidence demonstrates the presence of PRC2 complexes in various eukaryotic supergroups, suggesting conservation of the

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37

Blastyák, András, Rakesh K. Mishra, Francois Karch, and Henrik Gyurkovics. "Efficient and Specific Targeting of Polycomb Group Proteins Requires Cooperative Interaction between Grainyhead and Pleiohomeotic." Molecular and Cellular Biology 26, no. 4 (2006): 1434–44. http://dx.doi.org/10.1128/mcb.26.4.1434-1444.2006.

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ABSTRACT Specific targeting of the protein complexes formed by the Polycomb group of proteins is critically required to maintain the inactive state of a group of developmentally regulated genes. Although the role of DNA binding proteins in this process has been well established, it is still not understood how these proteins target the Polycomb complexes specifically to their response elements. Here we show that the grainyhead gene, which encodes a DNA binding protein, interacts with one such Polycomb response element of the bithorax complex. Grainyhead binds to this element in vitro. Moreover,

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38

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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Tang, Bo, Rui Sun, Dejie Wang, et al. "ZMYND8 preferentially binds phosphorylated EZH2 to promote a PRC2-dependent to -independent function switch in hypoxia-inducible factor–activated cancer." Proceedings of the National Academy of Sciences 118, no. 8 (2021): e2019052118. http://dx.doi.org/10.1073/pnas.2019052118.

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Both gene repressor (Polycomb-dependent) and activator (Polycomb-independent) functions of the Polycomb protein enhancer of zeste homolog 2 (EZH2) are implicated in cancer progression. EZH2 protein can be phosphorylated at various residues, such as threonine 487 (T487), by CDK1 kinase, and such phosphorylation acts as a Polycomb repressive complex 2 (PRC2) suppression “code” to mediate the gene repressor-to-activator switch of EZH2 functions. Here we demonstrate that the histone reader protein ZMYND8 is overexpressed in human clear cell renal cell carcinoma (ccRCC). ZMYND8 binds to EZH2, and t

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40

Ngubo, Mzwanele, Fereshteh Moradi, Caryn Y. Ito, and William L. Stanford. "Tissue-Specific Tumour Suppressor and Oncogenic Activities of the Polycomb-like Protein MTF2." Genes 14, no. 10 (2023): 1879. http://dx.doi.org/10.3390/genes14101879.

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The Polycomb repressive complex 2 (PRC2) is a conserved chromatin-remodelling complex that catalyses the trimethylation of histone H3 lysine 27 (H3K27me3), a mark associated with gene silencing. PRC2 regulates chromatin structure and gene expression during organismal and tissue development and tissue homeostasis in the adult. PRC2 core subunits are associated with various accessory proteins that modulate its function and recruitment to target genes. The multimeric composition of accessory proteins results in two distinct variant complexes of PRC2, PRC2.1 and PRC2.2. Metal response element-bind

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41

Faucheux, M., J. Y. Roignant, S. Netter, J. Charollais, C. Antoniewski, and L. Théodore. "batman Interacts with Polycomb and trithorax Group Genes and Encodes a BTB/POZ Protein That Is Included in a Complex Containing GAGA Factor." Molecular and Cellular Biology 23, no. 4 (2003): 1181–95. http://dx.doi.org/10.1128/mcb.23.4.1181-1195.2003.

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ABSTRACT Polycomb and trithorax group genes maintain the appropriate repressed or activated state of homeotic gene expression throughout Drosophila melanogaster development. We have previously identified the batman gene as a Polycomb group candidate since its function is necessary for the repression of Sex combs reduced. However, our present genetic analysis indicates functions of batman in both activation and repression of homeotic genes. The 127-amino-acid Batman protein is almost reduced to a BTB/POZ domain, an evolutionary conserved protein-protein interaction domain found in a large prote

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42

Veneti, Zoe, Kalliopi Gkouskou, and Aristides Eliopoulos. "Polycomb Repressor Complex 2 in Genomic Instability and Cancer." International Journal of Molecular Sciences 18, no. 8 (2017): 1657. http://dx.doi.org/10.3390/ijms18081657.

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43

Benoit, Y. D., M. B. Lepage, T. Khalfaoui, et al. "Polycomb repressive complex 2 impedes intestinal cell terminal differentiation." Journal of Cell Science 125, no. 14 (2012): 3454–63. http://dx.doi.org/10.1242/jcs.102061.

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44

Margueron, Raphaël, and Danny Reinberg. "The Polycomb complex PRC2 and its mark in life." Nature 469, no. 7330 (2011): 343–49. http://dx.doi.org/10.1038/nature09784.

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45

Shao, Zhaohui, Florian Raible, Ramin Mollaaghababa, et al. "Stabilization of Chromatin Structure by PRC1, a Polycomb Complex." Cell 98, no. 1 (1999): 37–46. http://dx.doi.org/10.1016/s0092-8674(00)80604-2.

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46

Cifuentes-Rojas, Catherine, Alfredo J. Hernandez, Kavitha Sarma, and Jeannie T. Lee. "Regulatory Interactions between RNA and Polycomb Repressive Complex 2." Molecular Cell 55, no. 2 (2014): 171–85. http://dx.doi.org/10.1016/j.molcel.2014.05.009.

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47

Zhang, Jisheng, Evan Bardot, and Elena Ezhkova. "Epigenetic regulation of skin: focus on the Polycomb complex." Cellular and Molecular Life Sciences 69, no. 13 (2012): 2161–72. http://dx.doi.org/10.1007/s00018-012-0920-x.

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Pherson, Michelle, Ziva Misulovin, Maria Gause, Kathie Mihindukulasuriya, Amanda Swain, and Dale Dorsett. "Polycomb repressive complex 1 modifies transcription of active genes." Science Advances 3, no. 8 (2017): e1700944. http://dx.doi.org/10.1126/sciadv.1700944.

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Lee, Stanley C. W., Belinda Phipson, Craig D. Hyland та ін. "Polycomb repressive complex 2 (PRC2) suppresses Eμ-myc lymphoma". Blood 122, № 15 (2013): 2654–63. http://dx.doi.org/10.1182/blood-2013-02-484055.

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Moritz, Lindsay E., and Raymond C. Trievel. "Structure, mechanism, and regulation of polycomb-repressive complex 2." Journal of Biological Chemistry 293, no. 36 (2017): 13805–14. http://dx.doi.org/10.1074/jbc.r117.800367.

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