Single Strand Annealing and ATP-independent Strand Exchange Activities of Yeast and Human DNA2: possible role in Ozaki fragment maturation
Abstract
The Dna2 protein is a multifunctional enzyme with 5'-3' DNA helicase, DNA-dependent ATPase, 3' exo/endonuclease, and 5' exo/endonuclease. The enzyme is highly specific for structures containing single-stranded flaps adjacent to duplex regions. We report here two novel activities of both the yeast and human Dna2 helicase/nuclease protein: single strand annealing and ATP-independent strand exchange on short duplexes. These activities are independent of ATPase/helicase and nuclease activities in that mutations eliminating either nuclease or ATPase/helicase do not inhibit strand annealing or strand exchange. ATP inhibits strand exchange. A model rationalizing the multiple catalytic functions of Dna2 and leading to its coordination with other enzymes in processing single-stranded flaps during DNA replication and repair is presented.
Additional Information
© 2006 the American Society for Biochemistry and Molecular Biology. Received for publication, May 23, 2006 , and in revised form, September 8, 2006. Originally published In Press as doi:10.1074/jbc.M604925200 on October 9, 2006 We thank Dr. Peter Snow and Dr. Bjoern Philipps of the Caltech Protein Expression Center for expression and purification of yeast and human Dna2. This work was supported in part by United States Public Health Service Grant GM25508 and grants from the Margaret E. Early Trust and the Research Management Group. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.Attached Files
Published - SASjbc06.pdf
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Additional details
- Eprint ID
- 6894
- Resolver ID
- CaltechAUTHORS:SASjcb06
- NIH
- GM25508
- Margaret E. Early Trust
- Research Management Group
- Created
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2006-12-31Created from EPrint's datestamp field
- Updated
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2021-11-08Created from EPrint's last_modified field