Dominant Saccharomyces cerevisiae msh6 Mutations Cause Increased Mispair Binding and Decreased Dissociation from Mispairs by Msh2-Msh6 in the Presence of ATP
Open Access
- 1 July 2002
- journal article
- Published by Elsevier
- Vol. 277 (28), 25545-25553
- https://doi.org/10.1074/jbc.m202282200
Abstract
No abstract availableKeywords
This publication has 66 references indexed in Scilit:
- hMSH3 and hMSH6 interact with PCNA and colocalize with it to replication fociGenes & Development, 2001
- Disruption of the helix-u-turn-helix motif of MutS protein: loss of subunit dimerization, mismatch binding and ATP hydrolysisJournal of Molecular Biology, 2001
- Composite Active Site of an ABC ATPaseMolecular Cell, 2001
- Mismatch Recognition and DNA-dependent Stimulation of the ATPase Activity of hMutSα Is Abolished by a Single Mutation in the hMSH6 SubunitPublished by Elsevier ,2000
- Analysis of yeast MSH2-MSH6 suggests that the initiation of mismatch repair can be separated into discrete stepsJournal of Molecular Biology, 2000
- Structural Biology of Rad50 ATPaseCell, 2000
- XtalView/Xfit—A Versatile Program for Manipulating Atomic Coordinates and Electron DensityJournal of Structural Biology, 1999
- Enhancement of MSH2–MSH3-mediated mismatch recognition by the yeast MLH1–PMS1 complexCurrent Biology, 1997
- Saccharomyces cerevisiae MSH2, a mispaired base recognition protein, also recognizes Holliday junctions in DNAJournal of Molecular Biology, 1997
- hMutSβ, a heterodimer of hMSH2 and hMSH3, binds to insertion/deletion loops in DNACurrent Biology, 1996