Role of histone H2A ubiquitination in Polycomb silencing Journal Article
| Authors: | Wang, H.; Wang, L.; Erdjument-Bromage, H.; Vidal, M.; Tempst, P.; Jones, R. S.; Zhang, Y. |
| Article Title: | Role of histone H2A ubiquitination in Polycomb silencing |
| Abstract: | 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. |
| Keywords: | controlled study; protein expression; unclassified drug; promoter region; dna-binding proteins; proto-oncogene proteins; nonhuman; ubiquitin; protein localization; animal cell; animals; animal tissue; gene; biology; ubiquitin protein ligase; embryo; cell line; animal experiment; rna interference; genetic transcription; homeodomain proteins; hela cell; hela cells; animalia; transcription factors; nuclear proteins; rna; dna; ubiquitination; amino acid sequence; molecular sequence data; enzyme analysis; histone; chromatin; gene repression; immunoprecipitation; multiprotein complexes; response elements; drosophila melanogaster; gene silencing; protein subunits; enzyme specificity; catalytic domain; histone h2a; histone h2b; bmi1 protein; repressor proteins; drosophila proteins; ubiquitin-protein ligases; histones; enzyme purification; enzymes; lysine; tissue; protein modification; forelimb; enzyme; nucleosome; nucleosomes; cells; promoter regions (genetics); covalent modification; humans; priority journal; article; polycomb silencing; hph2 protein; human polycomb repressive complex 1 like protein; polycomb protein; ring1 protein; ring2 protein; ubx gene |
| Journal Title: | Nature |
| Volume: | 431 |
| Issue: | 7010 |
| ISSN: | 0028-0836 |
| Publisher: | Nature Publishing Group |
| Date Published: | 2004-10-14 |
| Start Page: | 873 |
| End Page: | 878 |
| Language: | English |
| DOI: | 10.1038/nature02985 |
| PROVIDER: | scopus |
| PUBMED: | 15386022 |
| DOI/URL: | |
| Notes: | Nature -- Cited By (since 1996):582 -- Export Date: 16 June 2014 -- CODEN: NATUA -- Source: Scopus |
