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, Yoshizumi Ishino

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

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. Onthe 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.

Original languageEnglish
Pages (from-to)28023-28032
Number of pages10
JournalJournal of Biological Chemistry
Volume281
Issue number38
DOIs
Publication statusPublished - Sep 22 2006

Fingerprint

Pyrococcus furiosus
DNA Ligases
Proliferating Cell Nuclear Antigen
DNA
Enzyme activity
Enzymes
Ionic strength
DNA Replication
Joining
DNA Repair
Osmolar Concentration
Genetic Recombination
Repair
Salts
Amino Acids
Substrates

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Identification of a novel binding motif in Pyrococcus furiosus DNA ligase for the functional interaction with proliferating cell nuclear antigen. / Kiyonari, Shinichi; Takayama, Kohei; Nishida, Hirokazu; Ishino, Yoshizumi.

In: Journal of Biological Chemistry, Vol. 281, No. 38, 22.09.2006, p. 28023-28032.

Research output: Contribution to journalArticle

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AB - 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. Onthe 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.

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