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J. Biol. Chem., Vol. 281, Issue 38, 28023-28032, September 22, 2006

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Identification of a Novel Binding Motif in Pyrococcus furiosus DNA Ligase for the Functional Interaction with Proliferating Cell Nuclear Antigen^*

Shinichi Kiyonari, Kohei Takayama, Hirokazu Nishida, and Yoshizumi Ishino^¶1

From the Department of Genetic Resources Technology, Faculty of Agriculture, Kyushu University, and ^¶BIRD-Japan Science and Technology Agency, 6-10-1 Hakozaki, Fukuoka-shi, Fukuoka 812-8581, Japan and Central Research Laboratories, Hitachi Limited, 1-280 Higashi-koigakubo, Kokubunji, Tokyo 185-8581, Japan

DNA ligase is an essential enzyme for all organisms and catalyzes a nick-joining reaction in the final step of the DNA replication, repair, and recombination processes. Herein, we show the physical and functional interaction between DNA ligase and proliferating cell nuclear antigen (PCNA) from the hyperthermophilic Euryarchaea Pyrococcus furiosus. The stimulatory effect of P. furiosus PCNA on the enzyme activity of P. furiosus DNA ligase was observed not at low ionic strength, but at a high salt concentration, at which a DNA ligase alone cannot bind to a nicked DNA substrate. On the basis of mutational analyses, we identified the amino acid residues that are critical for PCNA binding in a loop structure located in the N-terminal DNA-binding domain of P. furiosus DNA ligase. We propose that the pentapeptide motif QKSFF is involved in the PCNA-interacting motifs, in which Gln and the first Phe are especially important for stable binding with PCNA.

Received for publication, April 10, 2006 , and in revised form, May 22, 2006.

^* This work was supported in part by the Japan Science and Technology Agency and by grants-in-aid from the Ministry of Education, Culture, Sports, Science, and Technology of Japan (to Y. I.). 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 and S2.

¹ Supported by the Human Frontier Science Program and the Hou-ansha Foundation. To whom correspondence should be addressed. Tel.: 81-92-642-4217; Fax: 81-92-642-3051; E-mail: ishino{at}agr.kyushu-u.ac.jp.

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