Identification of a novel binding motif in pyrococcus furiosus DNA ligase for the functional interaction with proliferating cell nuclear antigen

doi:10.1074/jbc.M603403200

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Papers In Press, published online ahead of print July 6, 2006
J. Biol. Chem, 10.1074/jbc.M603403200
Submitted on April 10, 2006
Revised on May 22, 2006
Accepted on July 6, 2006

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

Department of Genetic Resources Technology, Kyushu University, Fukuoka, Fukuoka 812-8581

Corresponding Author: ishino{at}agr.kyushu-u.ac.jp

DNA ligase is an essential enzyme for all organisms that 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 euryarchaeon, Pyrococcus furiosus. The stimulatory effect of P. furiosus PCNA (PfuPCNA) on the enzyme activity of DNA ligase (PfuLig) was observed not at a low ionic strength, but at a high salt concentration, at which a DNA ligase alone cannot bind to a nicked DNA substrate. Based on mutational analyses, we identified the amino acid residues that are critical for the PCNA binding in a loop structure located in the N-terminal DNA binding domain (DBD) of PfuLig. 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 the stable binding with PCNA.

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