Abstract：
:Ubiquitin-conjugating enzyme variant (UEV) proteins resemble ubiquitin-conjugating enzymes (E2s) but lack the defining E2 active-site residue. The MMS2-encoded UEV protein has been genetically implicated in error-free postreplicative DNA repair in Saccharomyces cerevisiae. We show that Mms2p forms a specific heteromeric complex with the UBC13-encoded E2 and is required for the Ubc13p-dependent assembly of polyubiquitin chains linked through lysine 63. A ubc13 yeast strain is UV sensitive, and single, double, and triple mutants of the UBC13, MMS2, and ubiquitin (ubiK63R) genes display a comparable phenotype. These findings support a model in which an Mms2p/Ubc13p complex assembles novel polyubiquitin chains for signaling in DNA repair, and they suggest that UEV proteins may act to increase diversity and selectivity in ubiquitin conjugation.
journal_name
Celljournal_title
Cellauthors
Hofmann RM,Pickart CMdoi
10.1016/s0092-8674(00)80575-9subject
Has Abstractpub_date
1999-03-05 00:00:00pages
645-53issue
5eissn
0092-8674issn
1097-4172pii
S0092-8674(00)80575-9journal_volume
96pub_type
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