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Role of histone H2A ubiquitination in Polycomb silencing

Covalent modification of histones is important in regulating chromatin dynamics and transcription. One example of such modification is ubiquitination, which mainly occurs on histones H2A and H2B. Although recent studies have uncovered the enzymes involved in histone H2B ubiquitination and a 'cross-t... Full description

Journal Title: Nature 2004-10-14, Vol.431 (7010), p.873-878
Main Author: Zhang, Yi
Other Authors: Wang, Hengbin , Wang, Liangjun , Erdjument-Bromage, Hediye , Vidal, Miguel , Tempst, Paul , Jones, Richard S
Format: Electronic Article Electronic Article
Language: English
Subjects:
Publisher: London: Nature Publishing
ID: ISSN: 0028-0836
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recordid: cdi_proquest_miscellaneous_746008667
title: Role of histone H2A ubiquitination in Polycomb silencing
format: Article
creator:
  • Zhang, Yi
  • Wang, Hengbin
  • Wang, Liangjun
  • Erdjument-Bromage, Hediye
  • Vidal, Miguel
  • Tempst, Paul
  • Jones, Richard S
subjects:
  • Amino Acid Sequence
  • animal structures
  • Animals
  • Biological and medical sciences
  • Catalytic Domain
  • Cell Line
  • DNA-Binding Proteins - chemistry
  • DNA-Binding Proteins - genetics
  • DNA-Binding Proteins - isolation & purification
  • DNA-Binding Proteins - metabolism
  • Drosophila
  • Drosophila melanogaster - genetics
  • Drosophila Proteins - genetics
  • embryonic structures
  • Fundamental and applied biological sciences. Psychology
  • Gene expression
  • Gene Silencing
  • HeLa Cells
  • Histones - metabolism
  • Homeodomain Proteins - genetics
  • Humans
  • Molecular and cellular biology
  • Molecular genetics
  • Molecular Sequence Data
  • Multiprotein Complexes
  • Nuclear Proteins - genetics
  • Nuclear Proteins - isolation & purification
  • Nuclear Proteins - metabolism
  • Nucleosomes - chemistry
  • Nucleosomes - metabolism
  • Polycomb Repressive Complex 1
  • Polycomb Repressive Complex 2
  • Polycomb-Group Proteins
  • Promoter Regions, Genetic - genetics
  • Protein Subunits - chemistry
  • Protein Subunits - genetics
  • Protein Subunits - isolation & purification
  • Protein Subunits - metabolism
  • Proto-Oncogene Proteins - genetics
  • Proto-Oncogene Proteins - isolation & purification
  • Proto-Oncogene Proteins - metabolism
  • Repressor Proteins - chemistry
  • Repressor Proteins - genetics
  • Repressor Proteins - isolation & purification
  • Repressor Proteins - metabolism
  • Response Elements - genetics
  • Transcription Factors - genetics
  • Transcription Factors - isolation & purification
  • Transcription Factors - metabolism
  • Ubiquitin - metabolism
  • Ubiquitin-Protein Ligases - chemistry
  • Ubiquitin-Protein Ligases - genetics
  • Ubiquitin-Protein Ligases - isolation & purification
  • Ubiquitin-Protein Ligases - metabolism
ispartof: Nature, 2004-10-14, Vol.431 (7010), p.873-878
description: Covalent modification of histones is important in regulating chromatin dynamics and transcription. One example of such modification is ubiquitination, which mainly occurs on histones H2A and H2B. Although recent studies have uncovered the enzymes involved in histone H2B ubiquitination and a 'cross-talk' between H2B ubiquitination and histone methylation, the responsible enzymes and the functions of H2A ubiquitination are unknown. Here we report the purification and functional characterization of an E3 ubiquitin ligase complex that is specific for histone H2A. The complex, termed hPRC1L (human Polycomb repressive complex 1-like), is composed of several Polycomb-group proteins including Ring1, Ring2, Bmi1 and HPH2. hPRC1L monoubiquitinates nucleosomal histone H2A at lysine 119. Reducing the expression of Ring2 results in a dramatic decrease in the level of ubiquitinated H2A in HeLa cells. Chromatin immunoprecipitation analysis demonstrated colocalization of dRing with ubiquitinated H2A at the PRE and promoter regions of the Drosophila Ubx gene in wing imaginal discs. Removal of dRing in SL2 tissue culture cells by RNA interference resulted in loss of H2A ubiquitination concomitant with derepression of Ubx. Thus, our studies identify the H2A ubiquitin ligase, and link H2A ubiquitination to Polycomb silencing.
language: eng
source:
identifier: ISSN: 0028-0836
fulltext: no_fulltext
issn:
  • 0028-0836
  • 1476-4687
url: Link


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titleRole of histone H2A ubiquitination in Polycomb silencing
creatorZhang, Yi ; Wang, Hengbin ; Wang, Liangjun ; Erdjument-Bromage, Hediye ; Vidal, Miguel ; Tempst, Paul ; Jones, Richard S
creatorcontribZhang, Yi ; Wang, Hengbin ; Wang, Liangjun ; Erdjument-Bromage, Hediye ; Vidal, Miguel ; Tempst, Paul ; Jones, Richard S
descriptionCovalent modification of histones is important in regulating chromatin dynamics and transcription. One example of such modification is ubiquitination, which mainly occurs on histones H2A and H2B. Although recent studies have uncovered the enzymes involved in histone H2B ubiquitination and a 'cross-talk' between H2B ubiquitination and histone methylation, the responsible enzymes and the functions of H2A ubiquitination are unknown. Here we report the purification and functional characterization of an E3 ubiquitin ligase complex that is specific for histone H2A. The complex, termed hPRC1L (human Polycomb repressive complex 1-like), is composed of several Polycomb-group proteins including Ring1, Ring2, Bmi1 and HPH2. hPRC1L monoubiquitinates nucleosomal histone H2A at lysine 119. Reducing the expression of Ring2 results in a dramatic decrease in the level of ubiquitinated H2A in HeLa cells. Chromatin immunoprecipitation analysis demonstrated colocalization of dRing with ubiquitinated H2A at the PRE and promoter regions of the Drosophila Ubx gene in wing imaginal discs. Removal of dRing in SL2 tissue culture cells by RNA interference resulted in loss of H2A ubiquitination concomitant with derepression of Ubx. Thus, our studies identify the H2A ubiquitin ligase, and link H2A ubiquitination to Polycomb silencing.
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descriptionCovalent modification of histones is important in regulating chromatin dynamics and transcription. One example of such modification is ubiquitination, which mainly occurs on histones H2A and H2B. Although recent studies have uncovered the enzymes involved in histone H2B ubiquitination and a 'cross-talk' between H2B ubiquitination and histone methylation, the responsible enzymes and the functions of H2A ubiquitination are unknown. Here we report the purification and functional characterization of an E3 ubiquitin ligase complex that is specific for histone H2A. The complex, termed hPRC1L (human Polycomb repressive complex 1-like), is composed of several Polycomb-group proteins including Ring1, Ring2, Bmi1 and HPH2. hPRC1L monoubiquitinates nucleosomal histone H2A at lysine 119. Reducing the expression of Ring2 results in a dramatic decrease in the level of ubiquitinated H2A in HeLa cells. Chromatin immunoprecipitation analysis demonstrated colocalization of dRing with ubiquitinated H2A at the PRE and promoter regions of the Drosophila Ubx gene in wing imaginal discs. Removal of dRing in SL2 tissue culture cells by RNA interference resulted in loss of H2A ubiquitination concomitant with derepression of Ubx. Thus, our studies identify the H2A ubiquitin ligase, and link H2A ubiquitination to Polycomb silencing.
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1animal structures
2Animals
3Biological and medical sciences
4Catalytic Domain
5Cell Line
6DNA-Binding Proteins - chemistry
7DNA-Binding Proteins - genetics
8DNA-Binding Proteins - isolation & purification
9DNA-Binding Proteins - metabolism
10Drosophila
11Drosophila melanogaster - genetics
12Drosophila Proteins - genetics
13embryonic structures
14Fundamental and applied biological sciences. Psychology
15Gene expression
16Gene Silencing
17HeLa Cells
18Histones - metabolism
19Homeodomain Proteins - genetics
20Humans
21Molecular and cellular biology
22Molecular genetics
23Molecular Sequence Data
24Multiprotein Complexes
25Nuclear Proteins - genetics
26Nuclear Proteins - isolation & purification
27Nuclear Proteins - metabolism
28Nucleosomes - chemistry
29Nucleosomes - metabolism
30Polycomb Repressive Complex 1
31Polycomb Repressive Complex 2
32Polycomb-Group Proteins
33Promoter Regions, Genetic - genetics
34Protein Subunits - chemistry
35Protein Subunits - genetics
36Protein Subunits - isolation & purification
37Protein Subunits - metabolism
38Proto-Oncogene Proteins - genetics
39Proto-Oncogene Proteins - isolation & purification
40Proto-Oncogene Proteins - metabolism
41Repressor Proteins - chemistry
42Repressor Proteins - genetics
43Repressor Proteins - isolation & purification
44Repressor Proteins - metabolism
45Response Elements - genetics
46Transcription Factors - genetics
47Transcription Factors - isolation & purification
48Transcription Factors - metabolism
49Ubiquitin - metabolism
50Ubiquitin-Protein Ligases - chemistry
51Ubiquitin-Protein Ligases - genetics
52Ubiquitin-Protein Ligases - isolation & purification
53Ubiquitin-Protein Ligases - metabolism
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1animal structures
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23Molecular Sequence Data
24Multiprotein Complexes
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37Protein Subunits - metabolism
38Proto-Oncogene Proteins - genetics
39Proto-Oncogene Proteins - isolation & purification
40Proto-Oncogene Proteins - metabolism
41Repressor Proteins - chemistry
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43Repressor Proteins - isolation & purification
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45Response Elements - genetics
46Transcription Factors - genetics
47Transcription Factors - isolation & purification
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50Ubiquitin-Protein Ligases - chemistry
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52Ubiquitin-Protein Ligases - isolation & purification
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abstractCovalent modification of histones is important in regulating chromatin dynamics and transcription. One example of such modification is ubiquitination, which mainly occurs on histones H2A and H2B. Although recent studies have uncovered the enzymes involved in histone H2B ubiquitination and a 'cross-talk' between H2B ubiquitination and histone methylation, the responsible enzymes and the functions of H2A ubiquitination are unknown. Here we report the purification and functional characterization of an E3 ubiquitin ligase complex that is specific for histone H2A. The complex, termed hPRC1L (human Polycomb repressive complex 1-like), is composed of several Polycomb-group proteins including Ring1, Ring2, Bmi1 and HPH2. hPRC1L monoubiquitinates nucleosomal histone H2A at lysine 119. Reducing the expression of Ring2 results in a dramatic decrease in the level of ubiquitinated H2A in HeLa cells. Chromatin immunoprecipitation analysis demonstrated colocalization of dRing with ubiquitinated H2A at the PRE and promoter regions of the Drosophila Ubx gene in wing imaginal discs. Removal of dRing in SL2 tissue culture cells by RNA interference resulted in loss of H2A ubiquitination concomitant with derepression of Ubx. Thus, our studies identify the H2A ubiquitin ligase, and link H2A ubiquitination to Polycomb silencing.
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pmid15386022
doi10.1038/nature02985
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