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17207499

Source:http://linkedlifedata.com/resource/pubmed/id/17207499

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pubmed-article:17207499pubmed:abstractTextMutS protein initiates mismatch repair with recognition of a non-Watson-Crick base-pair or base insertion/deletion site in DNA, and its interactions with DNA are modulated by ATPase activity. Here, we present a kinetic analysis of these interactions, including the effects of ATP binding and hydrolysis, reported directly from the mismatch site by 2-aminopurine fluorescence. When free of nucleotides, the Thermus aquaticus MutS dimer binds a mismatch rapidly (k(ON)=3 x 10(6) M(-1) s(-1)) and forms a stable complex with a half-life of 10 s (k(OFF)=0.07 s(-1)). When one or both nucleotide-binding sites on the MutS*mismatch complex are occupied by ATP, the complex remains fairly stable, with a half-life of 5-7 s (k(OFF)=0.1-0.14 s(-1)), although MutS(ATP) becomes incapable of (re-)binding the mismatch. When one or both nucleotide-binding sites on the MutS dimer are occupied by ADP, the MutS*mismatch complex forms rapidly (k(ON)=7.3 x 10(6) M(-1) s(-1)) and also dissociates rapidly, with a half-life of 0.4 s (k(OFF)=1.7 s(-1)). Integration of these MutS DNA-binding kinetics with previously described ATPase kinetics reveals that: (a) in the absence of a mismatch, MutS in the ADP-bound form engages in highly dynamic interactions with DNA, perhaps probing base-pairs for errors; (b) in the presence of a mismatch, MutS stabilized in the ATP-bound form releases the mismatch slowly, perhaps allowing for onsite interactions with downstream repair proteins; (c) ATP-bound MutS then moves off the mismatch, perhaps as a mobile clamp facilitating repair reactions at distant sites on DNA, until ATP is hydrolyzed (or dissociates) and the protein turns over.lld:pubmed
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pubmed-article:17207499pubmed:authorpubmed-author:Jacobs-Palmer...lld:pubmed
pubmed-article:17207499pubmed:authorpubmed-author:HingoraniManj...lld:pubmed
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pubmed-article:17207499pubmed:pagination1087-98lld:pubmed
pubmed-article:17207499pubmed:dateRevised2009-11-18lld:pubmed
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pubmed-article:17207499pubmed:year2007lld:pubmed
pubmed-article:17207499pubmed:articleTitleThe effects of nucleotides on MutS-DNA binding kinetics clarify the role of MutS ATPase activity in mismatch repair.lld:pubmed
pubmed-article:17207499pubmed:affiliationWesleyan University, Molecular Biology and Biochemistry Department, Middletown, CT 06459, USA.lld:pubmed
pubmed-article:17207499pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:17207499pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed
pubmed-article:17207499pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
pubmed-article:17207499pubmed:publicationTypeResearch Support, N.I.H., Extramurallld:pubmed
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