The yeast RAD52-dependent pathway is involved in DNA recombination and
double-strand break repair. Yeast ubiquitin-conjugating enzyme UBCS p
articipates in S- and M-phase cyclin degradation and mitotic control.
Using the human RAD52 protein as the ''bait'' in a yeast two-hybrid sy
stem, we have identified a human homolog of yeast UBCS, designated UBE
2I, that interacts with RAD52, RAD5I, p53, and a ubiquitin-like protei
n UBL1. These interactions are UBE2I-specific, since another DNA repai
r-related ubiquitin-conjugating enzyme, RAD6 (UBC2), does not interact
with these proteins. The interaction of UBE2I with RAD52 is mediated
by RAD52's self-association region. These results suggest that the RAD
52-dependent processes, cell cycle control, p53-mediated pathway(s), a
nd ubiquitination interact through human UBE2I. (C) 1996 Academic Pres
s, Inc.