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J. Biol. Chem., Vol. 282, Issue 27, 19917-19927, July 6, 2007

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Escherichia coli PriA Protein, Two Modes of DNA Binding and Activation of ATP Hydrolysis^*

Taku Tanaka, Toshimi Mizukoshi¹, Kaori Sasaki^¶, Daisuke Kohda^¶, and Hisao Masai²

From the Genome Dynamics Project, Tokyo Metropolitan Institute of Medical Science, Tokyo 113-8613, the Department of Structural Biology, Biomolecular Engineering Research Institute, Suita, Osaka 565-0874, and the ^¶Division of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan

Escherichia coli PriA protein plays crucial roles in processing of arrested replication forks. PriA serves as a sensor/stabilizer for an arrested replication fork and eventually promotes restart of DNA replication through assembly of a primosome. PriA carries a 3' terminus binding pocket required for its high affinity binding to a specific arrested fork as well as for its biological functions. We show here that PriA binds to DNA in a manner either dependent on or independent of 3' terminus recognition. The former mode of binding requires the 3' terminus binding pocket present at the N-terminal half of the 181-residue DNA binding domain and exhibits specific bipartite interaction on the template DNA. The latter mode is independent of the pocket function, but requires the C-terminal half of the same domain. ATP hydrolysis activity of PriA can be stimulated in vitro by either of the two binding modes. We propose architecture of PriA bound to various arrested replication fork structures and discuss its implication in helicase activation and ATP hydrolysis.

Received for publication, March 2, 2007 , and in revised form, April 20, 2007.

^* This work was supported in part by a grant-in-aid for Scientific Research on Priority Areas from the Ministry of Education, Culture, Sports, Science and Technology of Japan. 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.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1-S6 and Table S1.

¹ Present address: Basic Analytical Chemistry Group, Institute of Life Sciences, AJINOMOTO CO., INC., Kawasaki, 210-8681, Japan.

² To whom correspondence should be addressed. Tel.: 81-3-5685-2264; Fax: 81-3-5685-2932; E-mail: hmasai{at}rinshoken.or.jp.

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