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J. Biol. Chem., Vol. 281, Issue 50, 38466-38471, December 15, 2006

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Structure of the Escherichia coli DNA Polymerase III -HOT Proofreading Complex^*

Thomas W. Kirby, Scott Harvey, Eugene F. DeRose, Sergey Chalov, Anna K. Chikova^¶, Fred W. Perrino, Roel M. Schaaper^¶, Robert E. London¹, and Lars C. Pedersen

From the Laboratory of Structural Biology and the ^¶Laboratory of Molecular Genetics, NIEHS, National Institutes of Health, Research Triangle Park, North Carolina 27709 and Department of Biochemistry, Wake Forest University, Winston-Salem, North Carolina 27157

The subunit of Escherichia coli DNA polymerase III possesses 3'-exonucleolytic proofreading activity. Within the Pol III core, is tightly bound between the subunit (DNA polymerase) and subunit. Here, we present the crystal structure of in complex with HOT, the bacteriophage P1-encoded homolog of , at 2.1 Å resolution. The -HOT interface is defined by two areas of contact: an interaction of the previously unstructured N terminus of HOT with an edge of the central -sheet as well as interactions between HOT and the catalytically important helix 1-loop-helix 2 motif of . This structure provides insight into how HOT and, by implication, may stabilize the subunit, thus promoting efficient proofreading during chromosomal replication.

Received for publication, July 20, 2006

The atomic coordinates and structure factors (code 2IDO) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by the Intramural Research Program of the National Institutes of Health, by NIEHS, and by National Institutes of Health Grant GM069962 (to F. W. P.). 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.

¹ To whom correspondence should be addressed: Laboratory of Structural Biology, NIEHS, National Institutes of Health MR-01, 111 TW Alexander Dr., Research Triangle Park, NC 27709. Tel.: 919-541-4879; Fax: 919-541-5707; E-mail: london{at}niehs.nih.gov.

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