Hierarchical Recruitment of Polycomb Group Silencing Complexes
TLDR
Evidence is provided for the sequential binding of PcG proteins at a Polycomb response element (PRE) in proliferating cells in which the sequence-specific DNA binding Pho and Phol proteins directly recruit E(z)-containing complexes, which in turn methylate histone H3 at lysine 27 (H3mK27).About:
This article is published in Molecular Cell.The article was published on 2004-06-04 and is currently open access. It has received 573 citations till now. The article focuses on the topics: Ultrabithorax & Trithorax-group proteins.read more
Citations
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Journal ArticleDOI
The diverse functions of histone lysine methylation.
Cyrus Martin,Yi Zhang +1 more
TL;DR: Recent advances in understanding of how lysine methylation functions in these diverse biological processes are summarized, and questions that need to be addressed in the future are raised.
Journal ArticleDOI
Role of histone H2A ubiquitination in Polycomb silencing
Hengbin Wang,Liangjun Wang,Hediye Erdjument-Bromage,Miguel Vidal,Paul Tempst,Richard S. Jones,Yi Zhang +6 more
TL;DR: The purification and functional characterization of an E3 ubiquitin ligase complex that is specific for histone H2A is reported, and it is linked to Polycomb silencing, which is important in regulating chromatin dynamics and transcription.
Journal ArticleDOI
Genome Regulation by Polycomb and Trithorax Proteins
Bernd Schuettengruber,Daniel Chourrout,Michel Vervoort,Michel Vervoort,Benjamin Leblanc,Giacomo Cavalli +5 more
TL;DR: Polycomb group (PcG) and trithorax group (trxG) proteins are critical regulators of numerous developmental genes and recent work suggests that PcG-mediated gene silencing involves noncoding RNAs and the RNAi machinery.
Journal ArticleDOI
Polycomb silencers control cell fate, development and cancer
TL;DR: New insights are discussed into the possible mechanisms by which PcGs regulate cellular identity, and how these functions might be relevant during tumorigenesis are speculated.
Journal ArticleDOI
Mechanisms of Polycomb gene silencing: knowns and unknowns
TL;DR: New concepts include the existence of a Polycomb barrier to transcription elongation and the involvement of non-coding RNAs in the targeting of Polycomb complexes, which have an impact on the epigenetic programming of gene expression in many biological systems.
References
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Journal ArticleDOI
Role of Histone H3 Lysine 27 Methylation in Polycomb-Group Silencing
Ru Cao,Liangjun Wang,Hengbin Wang,Li Xia,Hediye Erdjument-Bromage,Paul Tempst,Richard S. Jones,Yi Zhang +7 more
TL;DR: The purification and characterization of an EED-EZH2 complex, the human counterpart of the Drosophila ESC-E(Z) complex, is reported, and it is demonstrated that the complex specifically methylates nucleosomal histone H3 at lysine 27 (H3-K27).
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Regulation of chromatin structure by site-specific histone H3 methyltransferases
Stephen Rea,Frank Eisenhaber,Dónal O'Carroll,Brian D. Strahl,Zu-Wen Sun,Manfred Schmid,Susanne Opravil,Karl Mechtler,Chris P. Ponting,C D Allis,Thomas Jenuwein +10 more
TL;DR: A functional interdependence of site-specific H3 tail modifications is revealed and a dynamic mechanism for the regulation of higher-order chromatin is suggested.
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Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein
TL;DR: The isolation of a multiprotein E(z) complex that contains extra sex combs, suppressor of zeste-12, and the histone binding proteins RbAp46/RbAp48 is reported, which possesses HMT activity with specificity for Lys 9 (K9) and Lys 27 (K27) of histone H3.
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Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites.
TL;DR: Histone H3 methylated in vitro by the E(Z)/ESC complex binds specifically to Polycomb protein, which is closely associated with Polycomb binding sites on polytene chromosomes but is also found in centric heterochromatin, chromosome 4, and telomeric sites.
Journal ArticleDOI
Histone methyltransferase activity of a Drosophila Polycomb group repressor complex
Jürg Müller,Craig M. Hart,Nicole J. Francis,Marcus L. Vargas,Aditya K. Sengupta,Aditya K. Sengupta,Brigitte Wild,Ellen L. Miller,Michael B. O'Connor,Michael B. O'Connor,Robert E. Kingston,Jeffrey A. Simon +11 more
TL;DR: This work purified an ESC-E(Z) complex from Drosophila embryos and found four major subunits: ESC, E(Z), NURF-55, and the PcG repressor, SU( Z)12, which methylates lysine-27 of histone H3.