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M604925200v1
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Papers In Press, published online ahead of print October 9, 2006
J. Biol. Chem, 10.1074/jbc.M604925200
Submitted on May 23, 2006
Revised on September 8, 2006
Accepted on October 9, 2006

Single-strand annealing and ATP-independent strand exchange activitiesof yeast and human DNA2: possible role in Okazaki fragment maturation

Taro Masuda-Sasa, Piotr Polaczek, and Judith L. Campbell

Divisions of Biology and Chemistry, California Institute of Technology, Pasadena, CA 91024

Corresponding Author: jcampbel{at}its.caltech.edu

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.


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T. Masuda-Sasa, P. Polaczek, X. P. Peng, L. Chen, and J. L. Campbell
Processing of G4 DNA by Dna2 Helicase/Nuclease and Replication Protein A (RPA) Provides Insights into the Mechanism of Dna2/RPA Substrate Recognition
J. Biol. Chem., September 5, 2008; 283(36): 24359 - 24373.
[Abstract] [Full Text] [PDF]


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