HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE ADVANCED SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Shibata, T. Articles by Shinagawa, H. Search for Related Content PubMed PubMed Citation Articles by Shibata, T. Articles by Shinagawa, H.

¹ Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan
² CREST, Japan Science and Technology Agency, Osaka 565-0871, Japan
³ The Tokyo Metropolitan Institute of Medical Science, Tokyo 113-8613, Japan
⁴ Graduate School of Integrated Science, Yokohama City University, Yokohama, 230-0045, Japan

Escherichia coli RecA protein plays a role in DNA homologous recombination, recombination repair, and the rescue of stalled or collapsed replication forks. The mgsA (rarA) gene encodes a highly conserved DNA-dependent ATPase, whose yeast orthologue, MGS1, plays a role in maintaining genomic stability. In this study, we show a functional relationship between mgsA and recA during DNA replication. The mgsA recA double mutant grows more slowly and has lower viability than a recA single mutant, but they are equally sensitive to UV-induced DNA damage. Mutations in mgsA and recA cause lethality in DNA polymerase I deficient cells, and suppress the temperature-dependent growth defect of dnaE486 (Pol III -catalytic subunit). Moreover, recAS25P, a novel recA allele identified in this work, does not complement the slow growth of mgsA recA cells or the lethality of polA12 recA, but is proficient in DNA repair, homologous recombination, SOS mutagenesis and SOS induction. These results suggest that RecA and MgsA are functionally redundant in rescuing stalled replication forks, and that the DNA repair and homologous recombination functions of RecA are separated from its function to maintain progression of replication fork.

^* Correspondence: E-mail: hishida{at}biken.osaka-u.ac.jp

This article has been cited by other articles:

				K. Fujimitsu, M. Su'etsugu, Y. Yamaguchi, K. Mazda, N. Fu, H. Kawakami, and T. Katayama Modes of Overinitiation, dnaA Gene Expression, and Inhibition of Cell Division in a Novel Cold-Sensitive hda Mutant of Escherichia coli J. Bacteriol., August 1, 2008; 190(15): 5368 - 5381. [Abstract] [Full Text] [PDF]

				K. Nagashima, Y. Kubota, T. Shibata, C. Sakaguchi, H. Shinagawa, and T. Hishida Degradation of Escherichia coli RecN Aggregates by ClpXP Protease and Its Implications for DNA Damage Tolerance J. Biol. Chem., October 13, 2006; 281(41): 30941 - 30946. [Abstract] [Full Text] [PDF]

				C. M. Roux, N. J. Booth, B. H. Bellaire, J. M. Gee, R. M. Roop II, M. E. Kovach, R. M. Tsolis, P. H. Elzer, and D. G. Ennis RecA and RadA Proteins of Brucella abortus Do Not Perform Overlapping Protective DNA Repair Functions following Oxidative Burst. J. Bacteriol., July 1, 2006; 188(14): 5187 - 5195. [Abstract] [Full Text] [PDF]