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Originally published In Press as doi:10.1074/jbc.M111854200 on January 24, 2002

J. Biol. Chem., Vol. 277, Issue 15, 13302-13311, April 12, 2002
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Human Exonuclease I Is Required for 5' and 3' Mismatch Repair*

Jochen GenschelDagger , Laura R. BazemoreDagger §, and Paul ModrichDagger §||

From the Dagger  Department of Biochemistry and § Howard Hughes Medical Institute, Duke University Medical Center, Durham, North Carolina 27710

We have partially purified a human activity that restores mismatch-dependent, bi-directional 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 hMutSalpha and hMutLalpha . However, excision directed by a 5' strand break requires hMutSalpha but can occur in absence of hMutLalpha . In systems comprised of pure components, the 5' to 3' hydrolytic activity of hEXOI is activated by hMutSalpha in a mismatch-dependent manner. These observations indicate a hydrolytic function for hEXOI in 5'-heteroduplex correction. The involvement of hEXOI in 3'-heteroduplex repair suggests that it has a regulatory/structural role in assembly of the 3'-excision complex or that the protein possesses a cryptic 3' to 5' hydrolytic activity.

* This work was supported by Grant GM45190 from NIGMS, National Institutes of Health.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Present address: Diosynth Research Triangle Park, Inc., 3000 Weston Parkway, Cary, NC 27513.

|| Investigator of the Howard Hughes Medical Institute. To whom correspondence should be addressed: Dept. of Biochemistry and Howard Hughes Medical Inst., Box 3711, Duke University Medical Center, Durham, NC 27710. Tel.: 919-684-2775; Fax: 919-681-7874; E-mail: modrich@biochem.duke.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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