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Papers In Press, published online ahead of print January 24, 2002
J. Biol. Chem, 10.1074/jbc.M111854200
Submitted on December 12, 2001
Revised on January 24, 2002
Accepted on January 24, 2002
Biochemistry and HHMI, Duke Univ. Medical Center, Durham, NC 27710
Corresponding Author: modrich{at}biochem.duke.edu
We have partially purified a human activity that restores mismatch-dependent, bidirectional excision to a human nuclear extract fraction depleted for one or more mismatch repair excision activities. Human EXOI co-purifies with the excision activity, and the purified activity can be replaced by near homogeneous recombinant hEXOI. Despite the reported 5' to 3' hydrolytic polarity of this activity, hEXOI participates in mismatch-provoked excision directed by a strand break located either 5' or 3' to the mispair. When the strand break that directs repair is located 3' to the mispair, hEXOI- and mismatch-dependent gap formation in excision-depleted extracts requires both hMutSa and hMutLa. However, excision directed by a 5’ strand break requires hMutSa but can occur in absence of hMutLa. In systems comprised of pure components, the 5' to 3' hydrolytic activity of hEXOI is activated by hMutSa in mismatch-dependent manner, and to a lesser extent by hMutLa in mismatch-independent fashion. These observations indicate a hydrolytic function for hEXOI in 5'-heteroduplex correction. The involvement of hEXOI in 3'-heteroduplex repair suggests that it has an important regulatory/structural role in assembly of the 3'-repair complex or that the protein possesses a cryptic 3' to 5' hydrolytic activity.
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