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The Polycomb‐associated protein Rybp is a ubiquitin binding protein
Author(s) -
Arrigoni Rachele,
Alam Steven L.,
Wamstad Joseph A.,
Bardwell Vivian J.,
Sundquist Wesley I.,
Schreiber-Agus Nicole
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.10.027
Subject(s) - ubiquitin , ubiquitin ligase , repressor , ubiquitin conjugating enzyme , microbiology and biotechnology , chemistry , histone , biochemistry , biology , gene , gene expression
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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