Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
47
pubmed:dateCreated
1994-12-28
pubmed:abstractText
MSH1 is a DNA-binding protein in yeast mitochondria that recognizes nucleotide mismatches in DNA and plays a role in mitochondrial mutation avoidance (Chi, W., and Kolodner, R. D. (1994) J. Biol. Chem. 269, 29984-29992). MSH1 exhibits an ATPase activity that hydrolyses approximately 1 ATP molecule/min in the absence of DNA. In this study, p3 show that DNA alters the pH dependence of the MSH1 ATPase and stimulates ATP hydrolysis at neutral pH. Using heteroduplex DNA containing mismatches with various affinity, we show an inverse correlation between the extent of ATPase stimulation by DNA and the binding affinity of MSH1 for the DNA effector. We also show that the presence of ATP increases the mismatch specificity of MSH1-DNA binding. Taken together, the observed interaction between the ATPase and the mismatch-binding activities suggests that MSH1 binds to ATP and mismatches with positive cooperativity. This interaction may provide a system for elucidating the role of ATP in mismatch recognition and repair.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
29993-7
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
The effect of DNA mismatches on the ATPase activity of MSH1, a protein in yeast mitochondria that recognizes DNA mismatches.
pubmed:affiliation
Division of Cellular and Molecular Biology, Dana-Farber Cancer Institute, Boston, Massachusetts 02115.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.