Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2052114 | FEBS Letters | 2006 | 9 Pages |
Abstract
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 PcG 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.
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Authors
Rachele Arrigoni, Steven L. Alam, Joseph A. Wamstad, Vivian J. Bardwell, Wesley I. Sundquist, Nicole Schreiber-Agus,