Biochemical basis for dominant mutations in the Saccharomyces cerevisiae MSH6 gene.

Abstract:

:Here, the ATP-binding, ATP hydrolysis, mispair-binding, sliding clamp formation, and Mlh1-Pms1 complex interaction properties of dominant mutant Msh2-Msh6 complexes have been characterized. The results demonstrate two mechanisms for dominance. In one, seen with the Msh6-S1036P and Msh6-G1067D mutant complexes, the mutant complex binds mispaired bases, is defective for ATP-induced sliding clamp formation and assembly of ternary complexes with Mlh1-Pms1, and occludes mispaired bases from other mismatch repair pathways. In the second, seen with the Msh6-G1142D complex, the mutant complex binds mispaired bases and is defective for ATP-induced sliding clamp formation but assembles ternary complexes with Mlh1-Pms1 that either occlude the mispaired base or prevent Mlh1-Pms1 from acting in alternate mismatch repair pathways.

authors

Hess MT,Mendillo ML,Mazur DJ,Kolodner RD

doi

10.1073/pnas.0510078103

keywords:

subject

Has Abstract

pub_date

2006-01-17 00:00:00

pages

558-63

issue

3

eissn

0027-8424

issn

1091-6490

pii

0510078103

journal_volume

103

pub_type

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