Affiliation:
1. Sealy Center for Molecular Science, University of Texas Medical Branch, Galveston, Texas
2. Institute of Genetics, Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary
Abstract
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.
Publisher
American Society for Microbiology
Subject
Cell Biology,Molecular Biology
Cited by
76 articles.
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