IndraLab

Statements


USP27X deubiquitinates Histone_H2B. 3 / 3
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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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"The requirement of ATXN7L3 for H2B deubiquitination by USP22, USP27x, and USP51 suggests that the ATXN7L3 zinc finger plays a role analogous to that of the Sgf11 zinc finger in docking human SAGA DUB [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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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."