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.
journal_name
Proc Natl Acad Sci U S Aauthors
Hess MT,Mendillo ML,Mazur DJ,Kolodner RDdoi
10.1073/pnas.0510078103keywords:
subject
Has Abstractpub_date
2006-01-17 00:00:00pages
558-63issue
3eissn
0027-8424issn
1091-6490pii
0510078103journal_volume
103pub_type
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