Role of histone H2A ubiquitination in Polycomb silencing

Hengbin Wang, Liangjun Wang, Hediye Erdjument-Bromage, Miguel Vidal, Paul Tempst, Richard S. Jones and Yi Zhang ()
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Hengbin Wang: University of North Carolina at Chapel Hill
Liangjun Wang: Southern Methodist University
Hediye Erdjument-Bromage: Memorial Sloan Kettering Cancer Center
Miguel Vidal: Centro de Investigaciones Biologicas
Paul Tempst: Memorial Sloan Kettering Cancer Center
Richard S. Jones: Southern Methodist University
Yi Zhang: University of North Carolina at Chapel Hill

Nature, 2004, vol. 431, issue 7010, 873-878

Abstract: Abstract Covalent modification of histones is important in regulating chromatin dynamics and transcription1,2. One example of such modification is ubiquitination, which mainly occurs on histones H2A and H2B3. Although recent studies have uncovered the enzymes involved in histone H2B ubiquitination4,5,6 and a ‘cross-talk’ between H2B ubiquitination and histone methylation7,8, 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.

Date: 2004
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DOI: 10.1038/nature02985

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