Role of Single-stranded DNA in Targeting REV1 to Primer Termini*
- Research Institute for Radiation Biology and Medicine, Hiroshima University, Hiroshima 734-8553, Japan
- 1 To whom correspondence should be addressed: Research Institute for Radiation Biology and Medicine, Hiroshima University, 1-2-3 Kasumi, Minamiku, Hiroshima 734-8553, Japan. Tel.: 81-82-257-5842; Fax: 81-82-257-5844; E-mail: kkamiya{at}hiroshima-u.ac.jp.
Abstract
Cellular functions of the REV1 gene have been conserved in evolution and appear important for maintaining genetic integrity through translesion DNA synthesis. This study documents a novel biochemical activity of human REV1 protein, due to higher affinity for single-stranded DNA (ssDNA) than the primer terminus. Preferential binding to long ssDNA regions of the template strand means that REV1 is targeted specifically to the included primer termini, a property not shared by other DNA polymerases, including human DNA polymerases α, β, and η. Furthermore, a mutant REV1 lacking N- and C-terminal domains, but catalytically active, lost this function, indicating that control is not due to the catalytic core. The novel activity of REV1 protein might imply a role for ssDNA in the regulation of translesion DNA synthesis.
Footnotes
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↵2 The abbreviations used are: pol, DNA polymerase; ssDNA, single-stranded DNA; BSA, bovine serum albumin.
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↵* This work was supported by grants from the Ministry of Education, Culture, Sports, Science, and Technology of Japan (to Y. M. and K. K.) and by the 21st Century Center of Excellence Program from the Ministry of Education, Culture, Sports, Science and Technology of Japan (to K. K.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
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The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. S1.
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- Received March 29, 2006.
- Revision received June 21, 2006.
- The American Society for Biochemistry and Molecular Biology, Inc.
