Associations of UBE2I with RAD52, UBL1, p53, and RAD51 proteins in a yeast two-hybrid system

Zhiyuan Shen, Paige E. Pardington-Purtymun, Jarmon C. Comeaux, Robert K. Moyzis, David J. Chen

Research output: Contribution to journalArticlepeer-review

127 Scopus citations

Abstract

The yeast RAD52-dependent pathway is involved in DNA recombination and double-strand break repair. Yeast ubiquitin-conjugating enzyme UBC9 participates in S- and M-phase cyclin degradation and mitotic control. Using the human RAD52 protein as the 'bait' in a yeast two-hybrid system, we have identified a human homolog of yeast UBC9, designated UBE2I, that interacts with RAD52, RAD51, p53, and a ubiquitin-like protein UBL1. These interactions are UBE2I-specific, since another DNA repair-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 RAD52-dependent processes, cell cycle control, p53- mediated pathway(s), and ubiquitination interact through human UBE2I.

Original languageEnglish (US)
Pages (from-to)183-186
Number of pages4
JournalGenomics
Volume37
Issue number2
DOIs
StatePublished - Oct 15 1996

ASJC Scopus subject areas

  • Genetics

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