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¹ Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, Noda, Chiba 278-8510, Japan
² R and D Division of Medical and Biological Laboratories, Co., Ltd, Ina, Nagano 396-0002, Japan
³ Cyclex, Co., Ltd, Ina, Nagano 396-0002, Japan

DNA polymerase lambda (Pol ) was recently identified as a new member of the family X of DNA polymerases. Here, we show that Pol directly binds to proliferating cell nuclear antigen (PCNA), an auxiliary protein for DNA replication and repair enzymes, both in vitro and in vivo. A pull-down assay using deletion mutants of Pol showed that the confined C-terminal region of Pol directly binds to PCNA. Furthermore, a synthetic peptide of 20-mers derived from the C-terminal region of Pol competes with full-length Pol for binding to PCNA. The residues between amino acids 518 and 537 of Pol are required for binding to PCNA, and are different from the consensus PCNA interacting motif (PIM). Pol associates with PCNA in vivo by immunoprecipitation analysis and EGFP-tagged Pol co-localizes with PCNA as spots within a nucleus using fluorescent microscopy. Through direct binding, PCNA suppressed the distributive nucleotidyltransferase activity of Pol . Pol µ, which also belongs to the family X of DNA polymerases, binds to PCNA by a pivotal amino acid residue.

^* Correspondence: E-mail: snoriko{at}rs.noda.tus.ac.jp

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