Journal
FEBS LETTERS
Volume 580, Issue 26, Pages 6233-6241Publisher
WILEY
DOI: 10.1016/j.febslet.2006.10.027
Keywords
Rybp; Ring1B; Polycomb group; ubiquitin; NZF; histone H2A
Funding
- NCI NIH HHS [CA71540, CA92558, R01 CA071540] Funding Source: Medline
- NIAID NIH HHS [R01 AI051174, AI51174] Funding Source: Medline
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The Rybp protein has been promoted as a Polycomb group (PcG)-associated protein, but its molecular function has remained elusive. Here we show that Rybp is a novel ubiquitin binding protein and is itself ubiquitinated. The Rybp interacting PeG protein Ring1B, a known ubiquitin E3 ligase, promotes Rybp ubiquitination. Moreover, one target of Rybp's ubiquitin binding domain appears to be ubiquitinated histone H2A; this histone is a substrate for Ring1B's E3 ligase activity in association with gene silencing processes. These findings on Rybp provide a further link between the ubiquitination system and PcG transcriptional repressors. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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