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J. Biol. Chem., Vol. 279, Issue 48, 50465-50471, November 26, 2004

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Crystal Structure of PriB, a Primosomal DNA Replication Protein of Escherichia coli^*

Jyung-Hurng Liu, Tsai-Wang Chang¶, Cheng-Yang Huang, Sue-Une Chen, Huey-Nan Wu, Ming-Chung Chang||**, and Chwan-Deng Hsiao

From the Graduate Institute of Life Sciences, National Defense Medical Center, Taipei, Taiwan 114, the Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan 115, and the Departments of ^¶Surgery and ^||Biochemistry, Medical College, National Cheng-Kung University, Tainan, Taiwan 701, Republic of China

PriB is one of the Escherichia coli X-type primosome proteins that are required for assembly of the primosome, a mobile multi-enzyme complex responsible for the initiation of DNA replication. Here we report the crystal structure of the E. coli PriB at 2.1 Å resolution by multi-wavelength anomalous diffraction using a mercury derivative. The polypeptide chain of PriB is structurally similar to that of single-stranded DNA-binding protein (SSB). However, the biological unit of PriB is a dimer, not a homotetramer like SSB. Electrophoretic mobility shift assays demonstrated that PriB binds single-stranded DNA and single-stranded RNA with comparable affinity. We also show that PriB binds single-stranded DNA with certain base preferences. Based on the PriB structural information and biochemical studies, we propose that the potential tetramer formation surface and several other regions of PriB may participate in protein-protein interaction during DNA replication. These findings may illuminate the role of PriB in X-type primosome assembly.

Received for publication, June 17, 2004 , and in revised form, August 31, 2004.

The atomic coordinates and structure factors (code 1V1Q) 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 research grants from Academia Sinica and National Science Council, Republic of China Grant NSC92-2311-B-00-088 (to C.-D. H.). 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.

^** To whom correspondence may be addressed. Tel.: 886-6-235-3535 (ext. 5513); Fax: 886-6-275-4697; E-mail: mcchang{at}mail.ncku.edu.tw. To whom correspondence may be addressed. Tel.: 886-2-2788-2743; Fax: 886-2-2782-6085; E-mail: mbhsiao{at}ccvax.sinica.edu.tw.

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