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Histone polyubiquitination

S. M., and Eisenman, R. N., Histone deacetylase 6 binds polyubiquitin through its zinc finger (PAZ domain) and copurifies with deubiquitinating enzymes, Proc. Natl. Acad. Scl USA, 2002, 99, 13425. [Pg.347]

In vivo ubiquitination is primarily restricted to histones H2A (uH2A) and H2B (uH2B) at Lysll9 and Lysl20, respectively (see Fig. 6) however, H3 (uH3) and HI (uHl) have also recently been shown to be modified at undefined sites [203,205,206]. In addition, H2A and H2B also display different patterns of ubiquitination as H2A has been found to be polyubiquitinated, and H2B only monoubiquitinated [207]. [Pg.257]

Sung, P., Prakash, S., and Prakash, L. (1988). The RAD6 protein of Saccharomyces cerevisiae polyubiquitinates histones, and its acidic domain mediates this activity. Genes Dev. 2, 1476-1485. [Pg.305]

See other pages where Histone polyubiquitination is mentioned: [Pg.208]    [Pg.338]    [Pg.248]    [Pg.227]    [Pg.257]    [Pg.231]    [Pg.62]   
See also in sourсe #XX -- [ Pg.228 ]



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