Initiator protein dimerization plays a key role in replication control of Vibrio cholerae chromosome 2
Identifieur interne : 001C18 ( Main/Exploration ); précédent : 001C17; suivant : 001C19Initiator protein dimerization plays a key role in replication control of Vibrio cholerae chromosome 2
Auteurs : Jyoti K. Jha [États-Unis] ; Rodolfo Ghirlando [États-Unis] ; Dhruba K. Chattoraj [États-Unis]Source :
- Nucleic Acids Research [ 0305-1048 ] ; 2014.
Descripteurs français
- KwdFr :
- ADN (biosynthèse), ADN (métabolisme), Chromosomes de bactérie, Liaison aux protéines, Multimérisation de protéines, Protéines bactériennes (), Protéines bactériennes (métabolisme), Protéines de liaison à l'ADN (), Protéines de liaison à l'ADN (métabolisme), Réplication de l'ADN, Structure tertiaire des protéines, Vibrio cholerae (génétique).
- MESH :
- biosynthèse : ADN.
- génétique : Vibrio cholerae.
- métabolisme : ADN, Protéines bactériennes, Protéines de liaison à l'ADN.
- Chromosomes de bactérie, Liaison aux protéines, Multimérisation de protéines, Protéines bactériennes, Protéines de liaison à l'ADN, Réplication de l'ADN, Structure tertiaire des protéines.
English descriptors
- KwdEn :
- Bacterial Proteins (chemistry), Bacterial Proteins (metabolism), Chromosomes, Bacterial, DNA (biosynthesis), DNA (metabolism), DNA Replication, DNA-Binding Proteins (chemistry), DNA-Binding Proteins (metabolism), Protein Binding, Protein Multimerization, Protein Structure, Tertiary, Vibrio cholerae (genetics).
- MESH :
- chemical , biosynthesis : DNA.
- chemical , chemistry : Bacterial Proteins, DNA-Binding Proteins.
- chemical , metabolism : Bacterial Proteins, DNA, DNA-Binding Proteins.
- genetics : Vibrio cholerae.
- Chromosomes, Bacterial, DNA Replication, Protein Binding, Protein Multimerization, Protein Structure, Tertiary.
Abstract
RctB, the initiator of replication of
Url:
DOI: 10.1093/nar/gku771
PubMed: 25159619
PubMed Central: 4176361
Affiliations:
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Le document en format XML
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Jha</name><affiliation wicri:level="2"><nlm:aff id="AFF1">Laboratory of Biochemistry and Molecular Biology, Center for Cancer Research, NCI, Bethesda, MD 20892, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Laboratory of Biochemistry and Molecular Biology, Center for Cancer Research, NCI, Bethesda, MD 20892</wicri:regionArea><placeName><region type="state">Maryland</region></placeName></affiliation></author><author><name sortKey="Ghirlando, Rodolfo" sort="Ghirlando, Rodolfo" uniqKey="Ghirlando R" first="Rodolfo" last="Ghirlando">Rodolfo Ghirlando</name><affiliation wicri:level="2"><nlm:aff id="AFF2">Laboratory of Molecular Biology, NIDDK, National Institutes of Health, Bethesda, MD 20892, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Laboratory of Molecular Biology, NIDDK, National Institutes of Health, Bethesda, MD 20892</wicri:regionArea><placeName><region type="state">Maryland</region></placeName></affiliation></author><author><name sortKey="Chattoraj, Dhruba K" sort="Chattoraj, Dhruba K" uniqKey="Chattoraj D" first="Dhruba K." last="Chattoraj">Dhruba K. Chattoraj</name><affiliation wicri:level="2"><nlm:aff id="AFF1">Laboratory of Biochemistry and Molecular Biology, Center for Cancer Research, NCI, Bethesda, MD 20892, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Laboratory of Biochemistry and Molecular Biology, Center for Cancer Research, NCI, Bethesda, MD 20892</wicri:regionArea><placeName><region type="state">Maryland</region></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">25159619</idno><idno type="pmc">4176361</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4176361</idno><idno type="RBID">PMC:4176361</idno><idno type="doi">10.1093/nar/gku771</idno><date when="2014">2014</date><idno type="wicri:Area/Pmc/Corpus">000F38</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000F38</idno><idno type="wicri:Area/Pmc/Curation">000F38</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000F38</idno><idno type="wicri:Area/Pmc/Checkpoint">001057</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">001057</idno><idno type="wicri:source">PubMed</idno><idno type="RBID">pubmed:25159619</idno><idno type="wicri:Area/PubMed/Corpus">001868</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001868</idno><idno type="wicri:Area/PubMed/Curation">001868</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001868</idno><idno type="wicri:Area/PubMed/Checkpoint">001872</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001872</idno><idno type="wicri:Area/Ncbi/Merge">000E80</idno><idno type="wicri:Area/Ncbi/Curation">000E80</idno><idno type="wicri:Area/Ncbi/Checkpoint">000E80</idno><idno type="wicri:doubleKey">0305-1048:2014:Jha J:initiator:protein:dimerization</idno><idno type="wicri:Area/Main/Merge">001C31</idno><idno type="wicri:Area/Main/Curation">001C18</idno><idno type="wicri:Area/Main/Exploration">001C18</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Initiator protein dimerization plays a key role in replication control of <italic>Vibrio cholerae</italic> chromosome 2</title><author><name sortKey="Jha, Jyoti K" sort="Jha, Jyoti K" uniqKey="Jha J" first="Jyoti K." last="Jha">Jyoti K. Jha</name><affiliation wicri:level="2"><nlm:aff id="AFF1">Laboratory of Biochemistry and Molecular Biology, Center for Cancer Research, NCI, Bethesda, MD 20892, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Laboratory of Biochemistry and Molecular Biology, Center for Cancer Research, NCI, Bethesda, MD 20892</wicri:regionArea><placeName><region type="state">Maryland</region></placeName></affiliation></author><author><name sortKey="Ghirlando, Rodolfo" sort="Ghirlando, Rodolfo" uniqKey="Ghirlando R" first="Rodolfo" last="Ghirlando">Rodolfo Ghirlando</name><affiliation wicri:level="2"><nlm:aff id="AFF2">Laboratory of Molecular Biology, NIDDK, National Institutes of Health, Bethesda, MD 20892, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Laboratory of Molecular Biology, NIDDK, National Institutes of Health, Bethesda, MD 20892</wicri:regionArea><placeName><region type="state">Maryland</region></placeName></affiliation></author><author><name sortKey="Chattoraj, Dhruba K" sort="Chattoraj, Dhruba K" uniqKey="Chattoraj D" first="Dhruba K." last="Chattoraj">Dhruba K. Chattoraj</name><affiliation wicri:level="2"><nlm:aff id="AFF1">Laboratory of Biochemistry and Molecular Biology, Center for Cancer Research, NCI, Bethesda, MD 20892, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Laboratory of Biochemistry and Molecular Biology, Center for Cancer Research, NCI, Bethesda, MD 20892</wicri:regionArea><placeName><region type="state">Maryland</region></placeName></affiliation></author></analytic><series><title level="j">Nucleic Acids Research</title><idno type="ISSN">0305-1048</idno><idno type="eISSN">1362-4962</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacterial Proteins (chemistry)</term><term>Bacterial Proteins (metabolism)</term><term>Chromosomes, Bacterial</term><term>DNA (biosynthesis)</term><term>DNA (metabolism)</term><term>DNA Replication</term><term>DNA-Binding Proteins (chemistry)</term><term>DNA-Binding Proteins (metabolism)</term><term>Protein Binding</term><term>Protein Multimerization</term><term>Protein Structure, Tertiary</term><term>Vibrio cholerae (genetics)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN (biosynthèse)</term><term>ADN (métabolisme)</term><term>Chromosomes de bactérie</term><term>Liaison aux protéines</term><term>Multimérisation de protéines</term><term>Protéines bactériennes ()</term><term>Protéines bactériennes (métabolisme)</term><term>Protéines de liaison à l'ADN ()</term><term>Protéines de liaison à l'ADN (métabolisme)</term><term>Réplication de l'ADN</term><term>Structure tertiaire des protéines</term><term>Vibrio cholerae (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>DNA</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Bacterial Proteins</term><term>DNA-Binding Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Bacterial Proteins</term><term>DNA</term><term>DNA-Binding Proteins</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>ADN</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Vibrio cholerae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Vibrio cholerae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ADN</term><term>Protéines bactériennes</term><term>Protéines de liaison à l'ADN</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Chromosomes, Bacterial</term><term>DNA Replication</term><term>Protein Binding</term><term>Protein Multimerization</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chromosomes de bactérie</term><term>Liaison aux protéines</term><term>Multimérisation de protéines</term><term>Protéines bactériennes</term><term>Protéines de liaison à l'ADN</term><term>Réplication de l'ADN</term><term>Structure tertiaire des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>RctB, the initiator of replication of <italic>Vibrio cholerae</italic> chromosome 2 (chr2), binds to the origin of replication to specific 12-mer sites both as a monomer and a dimer. Binding to 12-mers is essential for initiation. The monomers also bind to a second kind of site, 39-mers, which inhibits initiation. Mutations in <italic>rctB</italic> that reduce dimer binding increase monomer binding to 12-mers but decrease monomer binding to 39-mers. The mechanism of this paradoxical binding behavior has been unclear. Using deletion and alanine substitution mutants of RctB, we have now localized to a 71 amino acid region residues important for binding to the two kinds of DNA sites and for RctB dimerization. We find that the dimerization domain overlaps with both the DNA binding domains, explaining how changes in the dimerization domain can alter both kinds of DNA binding. Moreover, dimerization-defective mutants could be initiation-defective without apparent DNA binding defect. These results suggest that dimerization might be important for initiation beyond its role in controlling DNA binding. The finding that determinants of crucial initiator functions reside in a small region makes the region an attractive target for anti-<italic>V. cholerae</italic> drugs.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Watson, L C" uniqKey="Watson L">L.C. Watson</name></author><author><name sortKey="Kuchenbecker, K M" uniqKey="Kuchenbecker K">K.M. Kuchenbecker</name></author><author><name sortKey="Schiller, B J" uniqKey="Schiller B">B.J. Schiller</name></author><author><name sortKey="Gross, J D" uniqKey="Gross J">J.D. Gross</name></author><author><name sortKey="Pufall, M A" uniqKey="Pufall M">M.A. Pufall</name></author><author><name sortKey="Yamamoto, K R" uniqKey="Yamamoto K">K.R. Yamamoto</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Giraldo, R" uniqKey="Giraldo R">R. Giraldo</name></author><author><name sortKey="Fernandez Tornero, C" uniqKey="Fernandez Tornero C">C. 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Deniz</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Yamaichi, Y" uniqKey="Yamaichi Y">Y. Yamaichi</name></author><author><name sortKey="Duigou, S" uniqKey="Duigou S">S. Duigou</name></author><author><name sortKey="Shakhnovich, E A" uniqKey="Shakhnovich E">E.A. Shakhnovich</name></author><author><name sortKey="Waldor, M K" uniqKey="Waldor M">M.K. Waldor</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Maryland</li></region></list><tree><country name="États-Unis"><region name="Maryland"><name sortKey="Jha, Jyoti K" sort="Jha, Jyoti K" uniqKey="Jha J" first="Jyoti K." last="Jha">Jyoti K. Jha</name></region><name sortKey="Chattoraj, Dhruba K" sort="Chattoraj, Dhruba K" uniqKey="Chattoraj D" first="Dhruba K." last="Chattoraj">Dhruba K. Chattoraj</name><name sortKey="Ghirlando, Rodolfo" sort="Ghirlando, Rodolfo" uniqKey="Ghirlando R" first="Rodolfo" last="Ghirlando">Rodolfo Ghirlando</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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