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Genes to Cells (2004) 9, 523-531. doi:10.1111/j.1356-9597.2004.00747.x
© 2004 Blackwell Publishing or its licensors
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Interaction of hREV1 with three human Y-family DNA polymerases

Eiji Ohashi1, Yoshiki Murakumo2, Naoko Kanjo1, Jun-ichi Akagi3, Chikahide Masutani3,4, Fumio Hanaoka3,4 and Haruo Ohmori1,*

1 Institute for Virus Research, Kyoto University, 53 Shogoin-Kawaracho, Sakyo-ku, Kyoto 606-8507, Japan
2 Graduate School of Medicine, Nagoya University, 65 Tsurumai-cho, Showa-ku, Nagoya 466-8550, Japan
3 Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan
4 RIKEN, DRI and CREST, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan

Pol{kappa} is one of many DNA polymerases involved in translesion DNA synthesis (TLS). It belongs to the Y-family of polymerases along with Pol{eta}, Pol{iota} and hREV1. Unlike Pol{eta} encoded by the xeroderma pigmentosum variant (XPV) gene, Pol{kappa} is unable to bypass UV-induced DNA damage in vitro, but it is able to bypass benzo[a]pyrene (B[a]P)-adducted guanines accurately and efficiently. In an attempt to identify factor(s) targeting Pol{kappa} to its cognate DNA lesion(s), we searched for Pol{kappa}-interacting proteins by using the yeast two-hybrid assay. We found that Pol{kappa} interacts with a C-terminal region of hREV1. Pol{eta} and Pol{iota} were also found to interact with the same region of hREV1. The interaction between Pol{kappa} and hREV1 was confirmed by pull-down and co-immunoprecipitation assays. The C-terminal region of hREV1 is known to interact with hREV7, a non-catalytic subunit of Pol{zeta} that is another structurally unrelated TLS enzyme, and we show that Pol{kappa} and hREV7 bind to the same C-terminal region of hREV1. Thus, our results suggest that hREV1 plays a pivotal role in the multi-enzyme, multi-step process of translesion DNA synthesis.

Communicated by: Tadashi Yamamoto

* Correspondence: E-mail: hohmori{at}virus.kyoto-u.ac.jp




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