Initiator protein dimerization plays a key role in replication control of Vibrio cholerae chromosome 2.
Identifieur interne : 001868 ( PubMed/Corpus ); précédent : 001867; suivant : 001869Initiator protein dimerization plays a key role in replication control of Vibrio cholerae chromosome 2.
Auteurs : Jyoti K. Jha ; Rodolfo Ghirlando ; Dhruba K. ChattorajSource :
- Nucleic acids research [ 1362-4962 ] ; 2014.
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 Vibrio cholerae 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 rctB 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-V. cholerae drugs.
DOI: 10.1093/nar/gku771
PubMed: 25159619
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Chattoraj</name><affiliation><nlm:affiliation>Laboratory of Biochemistry and Molecular Biology, Center for Cancer Research, NCI, Bethesda, MD 20892, USA chattoraj@nih.gov.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:25159619</idno><idno type="pmid">25159619</idno><idno type="doi">10.1093/nar/gku771</idno><idno type="wicri:Area/PubMed/Corpus">001868</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001868</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Initiator protein dimerization plays a key role in replication control of Vibrio cholerae 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><nlm:affiliation>Laboratory of Biochemistry and Molecular Biology, Center for Cancer Research, NCI, Bethesda, MD 20892, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Ghirlando, Rodolfo" sort="Ghirlando, Rodolfo" uniqKey="Ghirlando R" first="Rodolfo" last="Ghirlando">Rodolfo Ghirlando</name><affiliation><nlm:affiliation>Laboratory of Molecular Biology, NIDDK, National Institutes of Health, Bethesda, MD 20892, USA.</nlm:affiliation></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><nlm:affiliation>Laboratory of Biochemistry and Molecular Biology, Center for Cancer Research, NCI, Bethesda, MD 20892, USA chattoraj@nih.gov.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Nucleic acids research</title><idno type="eISSN">1362-4962</idno><imprint><date when="2014" type="published">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="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="genetics" xml:lang="en"><term>Vibrio cholerae</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></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">RctB, the initiator of replication of Vibrio cholerae 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 rctB 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-V. cholerae drugs. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25159619</PMID><DateCompleted><Year>2015</Year><Month>01</Month><Day>20</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1362-4962</ISSN><JournalIssue CitedMedium="Internet"><Volume>42</Volume><Issue>16</Issue><PubDate><Year>2014</Year></PubDate></JournalIssue><Title>Nucleic acids research</Title><ISOAbbreviation>Nucleic Acids Res.</ISOAbbreviation></Journal><ArticleTitle>Initiator protein dimerization plays a key role in replication control of Vibrio cholerae chromosome 2.</ArticleTitle><Pagination><MedlinePgn>10538-49</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1093/nar/gku771</ELocationID><Abstract><AbstractText>RctB, the initiator of replication of Vibrio cholerae 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 rctB 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-V. cholerae drugs. </AbstractText><CopyrightInformation>Published by Oxford University Press on behalf of Nucleic Acids Research 2014. This work is written by (a) US Government employee(s) and is in the public domain in the US.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Jha</LastName><ForeName>Jyoti K</ForeName><Initials>JK</Initials><AffiliationInfo><Affiliation>Laboratory of Biochemistry and Molecular Biology, Center for Cancer Research, NCI, Bethesda, MD 20892, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ghirlando</LastName><ForeName>Rodolfo</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Laboratory of Molecular Biology, NIDDK, National Institutes of Health, Bethesda, MD 20892, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chattoraj</LastName><ForeName>Dhruba K</ForeName><Initials>DK</Initials><AffiliationInfo><Affiliation>Laboratory of Biochemistry and Molecular Biology, Center for Cancer Research, NCI, Bethesda, MD 20892, USA 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