IndraLab

Statements

USP27X deubiquitinates Histone_H2B. 3 / 3
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"The requirement of ATXN7L3 for H2B deubiquitination by USP22, USP27x, and USP51 suggests that all three use the ATXN7L3 zinc finger to dock the H2A and H2B acidic patch in a manner similar to that shown in the structure of the yeast DUB module bound to ubiquitinated nucleosomes."
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"Remarkably, this inhibitor also showed greater activity on USP22 than on two other DUBs, USP27x and USP51, that also deubiquitinate histone H2B and form complexes with two of the SAGA DUB module adaptor subunits."
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"Furthermore, USP27X mediates histone H2B deubiquitylation, which is critical for development (Weake et al, 2008)."
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