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Originally published In Press as doi:10.1074/jbc.M006828200 on November 17, 2000

J. Biol. Chem., Vol. 276, Issue 8, 5511-5517, February 23, 2001
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Lesion Bypass by the Escherichia coli DNA Polymerase V Requires Assembly of a RecA Nucleoprotein Filament*

Nina B. ReuvenDagger , Gali AradDagger , Alicja Z. Stasiak§, Andrzej Stasiak§, and Zvi LivnehDagger

From the Dagger  Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel and the § Laboratoire d'Analyse Ultrastructurale, Batiment de Biologie, Universite de Lausanne, CH-1015 Lausanne-Dorigny, Switzerland

Translesion replication is carried out in Escherichia coli by the SOS-inducible DNA polymerase V (UmuC), an error-prone polymerase, which is specialized for replicating through lesions in DNA, leading to the formation of mutations. Lesion bypass by pol V requires the SOS-regulated proteins UmuD' and RecA and the single-strand DNA-binding protein (SSB). Using an in vitro assay system for translesion replication based on a gapped plasmid carrying a site-specific synthetic abasic site, we show that the assembly of a RecA nucleoprotein filament is required for lesion bypass by pol V. This is based on the reaction requirements for stoichiometric amounts of RecA and for single-stranded gaps longer than 100 nucleotides and on direct visualization of RecA-DNA filaments by electron microscopy. SSB is likely to facilitate the assembly of the RecA nucleoprotein filament; however, it has at least one additional role in lesion bypass. ATPgamma S, which is known to strongly increase binding of RecA to DNA, caused a drastic inhibition of pol V activity. Lesion bypass does not require stoichiometric binding of UmuD' along RecA filaments. In summary, the RecA nucleoprotein filament, previously known to be required for SOS induction and homologous recombination, is also a critical intermediate in translesion replication.

* This research was supported by Grants 96-00448 and 1999141 from the United States-Israel Binational Science Foundation. Grant 31-58841.99 from the Swiss National Science Foundation, and a grant from the Human Science Frontiers Program (to A. S. and A. Z. S.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Incumbent of The Maxwell Ellis Professorial Chair in Biomedical Research. To whom all correspondence should be addressed: Dept. of Biological Chemistry, Weizmann Inst. of Science, Rehovot 76100, Israel. Tel.: 972-8-934-3203; Fax: 972-8-934-4169; E-mail: zvi.livneh@weizmann.ac.il.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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