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Relevant bibliographies by topics / Complexe polycomb

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Journal articles

Academic literature on the topic 'Complexe polycomb'

Author: Grafiati

Published: 31 August 2024

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Journal articles on the topic "Complexe polycomb"

1

Dong, Guan-Jun, Jia-Le Xu, Yu-Ruo Qi, Zi-Qiao Yuan, and Wen Zhao. "Critical Roles of Polycomb Repressive Complexes in Transcription and Cancer." International Journal of Molecular Sciences 23, no. 17 (2022): 9574. http://dx.doi.org/10.3390/ijms23179574.

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Polycomp group (PcG) proteins are members of highly conserved multiprotein complexes, recognized as gene transcriptional repressors during development and shown to play a role in various physiological and pathological processes. PcG proteins consist of two Polycomb repressive complexes (PRCs) with different enzymatic activities: Polycomb repressive complexes 1 (PRC1), a ubiquitin ligase, and Polycomb repressive complexes 2 (PRC2), a histone methyltransferase. Traditionally, PRCs have been described to be associated with transcriptional repression of homeotic genes, as well as gene transcriptio

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2

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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3

Meseure, D., S. Vacher, M. Trassard, et al. "Rôles du complexe répresseur Polycomb EZH2/CBX7 et du long ARN non codant ANRIL dans l’induction des mécanismes de silencing épigénétique. Implications thérapeutiques potentielles dans les carcinomes mammaires de type triple négatif." Annales de Pathologie 31, no. 5 (2011): S125. http://dx.doi.org/10.1016/j.annpat.2011.09.021.

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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

Zhou, Haining, Chad B. Stein, Tiasha A. Shafiq, et al. "Rixosomal RNA degradation contributes to silencing of Polycomb target genes." Nature 604, no. 7904 (2022): 167–74. http://dx.doi.org/10.1038/s41586-022-04598-0.

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AbstractPolycomb repressive complexes 1 and 2 (PRC1 and PRC2) are histone-modifying and -binding complexes that mediate the formation of facultative heterochromatin and are required for silencing of developmental genes and maintenance of cell fate1–3. Multiple pathways of RNA decay work together to establish and maintain heterochromatin in fission yeast, including a recently identified role for a conserved RNA-degradation complex known as the rixosome or RIX1 complex4–6. Whether RNA degradation also has a role in the stability of mammalian heterochromatin remains unknown. Here we show that the

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6

MA, Ke-Xue, and Xing-Zi XI. "Polycomb group protein complexes." Hereditas (Beijing) 31, no. 10 (2009): 977–81. http://dx.doi.org/10.3724/sp.j.1005.2009.00977.

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7

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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8

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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9

Lund, Anders H., and Maarten van Lohuizen. "Polycomb complexes and silencing mechanisms." Current Opinion in Cell Biology 16, no. 3 (2004): 239–46. http://dx.doi.org/10.1016/j.ceb.2004.03.010.

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10

Schwartz, Yuri B., and Vincenzo Pirrotta. "Polycomb complexes and epigenetic states." Current Opinion in Cell Biology 20, no. 3 (2008): 266–73. http://dx.doi.org/10.1016/j.ceb.2008.03.002.

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