Premium
Interaction of hREV1 with three human Y‐family DNA polymerases
Author(s) -
Ohashi Eiji,
Murakumo Yoshiki,
Kanjo Naoko,
Akagi Junichi,
Masutani Chikahide,
Hanaoka Fumio,
Ohmori Haruo
Publication year - 2004
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/j.1356-9597.2004.00747.x
Subject(s) - biology , xeroderma pigmentosum , dna polymerase , dna , protein subunit , microbiology and biotechnology , polymerase , dna damage , immunoprecipitation , biochemistry , genetics , gene
Polκ is one of many DNA polymerases involved in translesion DNA synthesis (TLS). It belongs to the Y‐family of polymerases along with Polη, Polι and hREV1. Unlike Polη encoded by the xeroderma pigmentosum variant ( XPV ) gene, Polκ 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 Polκ to its cognate DNA lesion(s), we searched for Polκ‐interacting proteins by using the yeast two‐hybrid assay. We found that Polκ interacts with a C‐terminal region of hREV1. Polη and Polι were also found to interact with the same region of hREV1. The interaction between Polκ 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 Polζ that is another structurally unrelated TLS enzyme, and we show that Polκ 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.