Functional overlap between RecA and MgsA (RarA) in the rescue of stalled replication forks in Escherichia coli
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 stabilit...
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Veröffentlicht in: | Genes to cells : devoted to molecular & cellular mechanisms 2005-03, Vol.10 (3), p.181-191 |
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creator | Shibata, Tatsuya Hishida, Takashi Kubota, Yoshino Han, Yong‐Woon Iwasaki, Hiroshi Shinagawa, Hideo |
description | 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 α‐catalytic subunit). Moreover, recAS25P, a novel recA allele identified in this work, does not complement the slow growth of ΔmgsA ΔrecA cells or the lethality of polA12 ΔrecA, 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. |
doi_str_mv | 10.1111/j.1365-2443.2005.00831.x |
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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 α‐catalytic subunit). Moreover, recAS25P, a novel recA allele identified in this work, does not complement the slow growth of ΔmgsA ΔrecA cells or the lethality of polA12 ΔrecA, but is proficient in DNA repair, homologous recombination, SOS mutagenesis and SOS induction. 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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 α‐catalytic subunit). Moreover, recAS25P, a novel recA allele identified in this work, does not complement the slow growth of ΔmgsA ΔrecA cells or the lethality of polA12 ΔrecA, 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.</description><subject>Adenosine Triphosphatases - genetics</subject><subject>Adenosine Triphosphatases - metabolism</subject><subject>DNA Helicases - genetics</subject><subject>DNA Helicases - metabolism</subject><subject>DNA Replication - physiology</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins - genetics</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Gene Expression Regulation, Bacterial</subject><subject>Mutation</subject><subject>Rec A Recombinases - genetics</subject><subject>Rec A Recombinases - metabolism</subject><issn>1356-9597</issn><issn>1365-2443</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkMFKAzEQhoMoWquvIDmJHnZNmqTZBS-ltCooQtFzyKYTm5ru1mTX2rd31xa9OpcZkm_-gQ8hTElK27pZppQNRTLgnKUDQkRKSMZo-nWAer8fh90shkkucnmCTmNcEkLZgIhjdEKF5IyTvIfKaVOa2lWl9rj6hOD1GhdQbwBKPAMzwrqc46e3OMJXMx1G19iVuF4ADhBNA7iyONbae5i3L2vvjO6ysK3Ce-zQSTQLCM4snMam8u4MHVntI5zvex-9Ticv4_vk8fnuYTx6TIwQkiaa55SA0UwYmuWD3Fo5zwsAS0BmFgQQW3DJCSHMSC50YS0bGiklBygYMNZHl7vcdag-Goi1WrlowHtdQtVERWXGsiETLZjtQBOqGANYtQ5upcNWUaI612qpOqWqU6o61-rHtfpqVy_2N5piBfO_xb3cFrjdARvnYfvvYHX3Mm4H9g2UiY1z</recordid><startdate>200503</startdate><enddate>200503</enddate><creator>Shibata, Tatsuya</creator><creator>Hishida, Takashi</creator><creator>Kubota, Yoshino</creator><creator>Han, Yong‐Woon</creator><creator>Iwasaki, Hiroshi</creator><creator>Shinagawa, Hideo</creator><general>Blackwell Science Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>200503</creationdate><title>Functional overlap between RecA and MgsA (RarA) in the rescue of stalled replication forks in Escherichia coli</title><author>Shibata, Tatsuya ; Hishida, Takashi ; Kubota, Yoshino ; Han, Yong‐Woon ; Iwasaki, Hiroshi ; Shinagawa, Hideo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5571-a4910eca35c18929ff7d9beef0e78fe5e0fb4740003c745abff36c7774eeb3e33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Adenosine Triphosphatases - genetics</topic><topic>Adenosine Triphosphatases - metabolism</topic><topic>DNA Helicases - genetics</topic><topic>DNA Helicases - metabolism</topic><topic>DNA Replication - physiology</topic><topic>Escherichia coli</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli Proteins - genetics</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Gene Expression Regulation, Bacterial</topic><topic>Mutation</topic><topic>Rec A Recombinases - genetics</topic><topic>Rec A Recombinases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shibata, Tatsuya</creatorcontrib><creatorcontrib>Hishida, Takashi</creatorcontrib><creatorcontrib>Kubota, Yoshino</creatorcontrib><creatorcontrib>Han, Yong‐Woon</creatorcontrib><creatorcontrib>Iwasaki, Hiroshi</creatorcontrib><creatorcontrib>Shinagawa, Hideo</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Genes to cells : devoted to molecular & cellular mechanisms</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shibata, Tatsuya</au><au>Hishida, Takashi</au><au>Kubota, Yoshino</au><au>Han, Yong‐Woon</au><au>Iwasaki, Hiroshi</au><au>Shinagawa, Hideo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional overlap between RecA and MgsA (RarA) in the rescue of stalled replication forks in Escherichia coli</atitle><jtitle>Genes to cells : devoted to molecular & cellular mechanisms</jtitle><addtitle>Genes Cells</addtitle><date>2005-03</date><risdate>2005</risdate><volume>10</volume><issue>3</issue><spage>181</spage><epage>191</epage><pages>181-191</pages><issn>1356-9597</issn><eissn>1365-2443</eissn><abstract>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 α‐catalytic subunit). Moreover, recAS25P, a novel recA allele identified in this work, does not complement the slow growth of ΔmgsA ΔrecA cells or the lethality of polA12 ΔrecA, but is proficient in DNA repair, homologous recombination, SOS mutagenesis and SOS induction. 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subjects | Adenosine Triphosphatases - genetics Adenosine Triphosphatases - metabolism DNA Helicases - genetics DNA Helicases - metabolism DNA Replication - physiology Escherichia coli Escherichia coli - enzymology Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Gene Expression Regulation, Bacterial Mutation Rec A Recombinases - genetics Rec A Recombinases - metabolism |
title | Functional overlap between RecA and MgsA (RarA) in the rescue of stalled replication forks in Escherichia coli |
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