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Papers In Press, published online ahead of print September 27, 2005
Biochemistry and HHMI, Duke Univ. Medical Center, Durham, NC 27710
Corresponding Author: modrich{at}biochem.duke.edu
Bidirectional mismatch repair directed by a strand break located 3' or 5' to the mispair has been reconstituted using seven purified human activities: MutSa, MutLa, EXOI, RPA, PCNA, RFC, and DNA polymerase d. In addition to DNA polymerase d, PCNA, RFC, and RPA, 5'-directed repair depends on MutSa and EXOI, whereas 3'-directed mismatch correction also requires MutLa. The repair reaction displays specificity for DNA polymerase d, an effect that presumably reflects interactions with other repair activities. Since previous studies have suggested potential involvement of the editing function of a replicative polymerase in mismatch-provoked excision, we have evaluated possible participation of DNA polymerase d in the excision step of repair. RFC and PCNA dramatically activate polymerase d-mediated hydrolysis of a primer-template. Nevertheless, the contribution of the polymerase to mismatch-provoked excision is very limited, both in the purified system and in HeLa extracts, as judged by in vitro assay using nicked circular heteroplex DNAs. Thus, excision and repair in the purified system containing polymerase d are reduced 10-fold upon omission of EXOI or by substitution of a catalytically dead form of the exonuclease. Furthermore aphidicolin inhibits both 3'- and 5'-directed excision in HeLa nuclear extracts by only 20-30%. Although this modest inhibition could be due to nonspecific effects, it may indicate limited dependence of bidirectional excision on an aphidicolin-sensitive DNA polymerase.
J. Biol. Chem, 10.1074/jbc.M509701200
Submitted on September 2, 2005
Accepted on September 26, 2005
Human mismatch repair: Reconstitution of a nick-directed bidirectional reaction
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