Complex formation of yeast Rev1 and Rev7 proteins: A novel role for the polymerase-associated domain

Narottam Acharya, Lajos Haracska, Robert E. Johnson, Ildiko Unk, Satya Prakash, Louise Prakash

Research output: Contribution to journalArticle

60 Scopus citations

Abstract

The Rev1 protein of Saccharomyces cerevisiae functions in translesion synthesis (TLS) together with DNA polymerase (Pol) ζ, which is comprised of the Rev3 catalytic and the Rev7 accessory subunits. Rev1, a member of the Y family of Pols, differs from other members in its high degree of specificity for incorporating a C opposite template G as well as opposite an abasic site. Although Rev1 is indispensable for Polζ-dependent TLS, its DNA synthetic activity is not required for many of the Polζ-dependent lesion bypass events. This observation has suggested a structural role for Rev1 in this process. Here we show that in yeast, Rev1 forms a stable complex with Rev7, and the two proteins copurify. Importantly, the polymerase-associated domain (PAD) of Rev1 mediates its binding to Rev7. These observations reveal a novel role for the PAD region of Rev1 in protein-protein interactions, and they raise the possibility of a similar involvement of the PAD of other Y family Pols in protein-protein interactions. We discuss the possible roles of Rev1 versus the Rev1-Rev7 complex in TLS.

Original languageEnglish (US)
Pages (from-to)9734-9740
Number of pages7
JournalMolecular and cellular biology
Volume25
Issue number21
DOIs
StatePublished - Nov 1 2005

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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