IciA protein, a specific inhibitor of initiation of Escherichia coli chromosomal replication.
Identifieur interne : 002967 ( PubMed/Corpus ); précédent : 002966; suivant : 002968IciA protein, a specific inhibitor of initiation of Escherichia coli chromosomal replication.
Auteurs : D S Hwang ; B. Thöny ; A. KornbergSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1992.
English descriptors
- KwdEn :
- Bacterial Proteins (biosynthesis), Bacterial Proteins (genetics), Bacterial Proteins (metabolism), Base Sequence, Chromosomes, Bacterial, DNA Replication, DNA, Bacterial (biosynthesis), DNA-Binding Proteins (biosynthesis), DNA-Binding Proteins (genetics), DNA-Binding Proteins (metabolism), Electrophoresis, Polyacrylamide Gel, Escherichia coli (genetics), Escherichia coli Proteins, Molecular Sequence Data, Plasmids.
- MESH :
- chemical , biosynthesis : Bacterial Proteins, DNA, Bacterial, DNA-Binding Proteins.
- chemical , genetics : Bacterial Proteins, DNA-Binding Proteins.
- chemical , metabolism : Bacterial Proteins, DNA-Binding Proteins.
- genetics : Escherichia coli.
- Base Sequence, Chromosomes, Bacterial, DNA Replication, Electrophoresis, Polyacrylamide Gel, Escherichia coli Proteins, Molecular Sequence Data, Plasmids.
Abstract
Specific binding of IciA protein to the 13-mers in the origin of a minichromosome (oriC) inhibits initiation of replication in vitro by blocking the opening of this region effected by the initiator DnaA protein (Hwang, D.S., and Kornberg, A. (1990) Cell 63, 325-331). Isolation of the iciA gene (Thöny, B., Hwang, D.S., Fradkin, L., and Kornberg, A. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 4066-4070) has made possible the construction of an IciA-overproducing strain, which in turn has simplified the isolation of a large quantity of the protein, indistinguishable from that of the wild-type strain. Based on sedimentation and gel filtration, the IciA protein is an elongated dimer of a 33.4-kDa subunit. The specific binding of IciA protein to the 13-mers was stable for 2 h at 30 degrees C. The amounts of IciA protein, detected by immunoassays, increased 4-fold compared with levels (about 100 dimers) in log-phase cells whereas levels of DnaA protein decreased upon entry of cells into the stationary phase.
PubMed: 1733927
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pubmed:1733927Le document en format XML
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Kornberg</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1992">1992</date><idno type="RBID">pubmed:1733927</idno><idno type="pmid">1733927</idno><idno type="wicri:Area/PubMed/Corpus">002967</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002967</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">IciA protein, a specific inhibitor of initiation of Escherichia coli chromosomal replication.</title><author><name sortKey="Hwang, D S" sort="Hwang, D S" uniqKey="Hwang D" first="D S" last="Hwang">D S Hwang</name><affiliation><nlm:affiliation>Department of Biochemistry, Stanford University School of Medicine, California 94305-5307.</nlm:affiliation></affiliation></author><author><name sortKey="Thony, B" sort="Thony, B" uniqKey="Thony B" first="B" last="Thöny">B. Thöny</name></author><author><name sortKey="Kornberg, A" sort="Kornberg, A" uniqKey="Kornberg A" first="A" last="Kornberg">A. 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(1990) Cell 63, 325-331). Isolation of the iciA gene (Thöny, B., Hwang, D.S., Fradkin, L., and Kornberg, A. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 4066-4070) has made possible the construction of an IciA-overproducing strain, which in turn has simplified the isolation of a large quantity of the protein, indistinguishable from that of the wild-type strain. Based on sedimentation and gel filtration, the IciA protein is an elongated dimer of a 33.4-kDa subunit. The specific binding of IciA protein to the 13-mers was stable for 2 h at 30 degrees C. The amounts of IciA protein, detected by immunoassays, increased 4-fold compared with levels (about 100 dimers) in log-phase cells whereas levels of DnaA protein decreased upon entry of cells into the stationary phase.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1733927</PMID><DateCompleted><Year>1992</Year><Month>03</Month><Day>03</Day></DateCompleted><DateRevised><Year>2014</Year><Month>11</Month><Day>20</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>267</Volume><Issue>4</Issue><PubDate><Year>1992</Year><Month>Feb</Month><Day>05</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J. Biol. Chem.</ISOAbbreviation></Journal><ArticleTitle>IciA protein, a specific inhibitor of initiation of Escherichia coli chromosomal replication.</ArticleTitle><Pagination><MedlinePgn>2209-13</MedlinePgn></Pagination><Abstract><AbstractText>Specific binding of IciA protein to the 13-mers in the origin of a minichromosome (oriC) inhibits initiation of replication in vitro by blocking the opening of this region effected by the initiator DnaA protein (Hwang, D.S., and Kornberg, A. (1990) Cell 63, 325-331). Isolation of the iciA gene (Thöny, B., Hwang, D.S., Fradkin, L., and Kornberg, A. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 4066-4070) has made possible the construction of an IciA-overproducing strain, which in turn has simplified the isolation of a large quantity of the protein, indistinguishable from that of the wild-type strain. Based on sedimentation and gel filtration, the IciA protein is an elongated dimer of a 33.4-kDa subunit. The specific binding of IciA protein to the 13-mers was stable for 2 h at 30 degrees C. The amounts of IciA protein, detected by immunoassays, increased 4-fold compared with levels (about 100 dimers) in log-phase cells whereas levels of DnaA protein decreased upon entry of cells into the stationary phase.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hwang</LastName><ForeName>D S</ForeName><Initials>DS</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Stanford University School of Medicine, California 94305-5307.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Thöny</LastName><ForeName>B</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Kornberg</LastName><ForeName>A</ForeName><Initials>A</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004269">DNA, Bacterial</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004268">DNA-Binding Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C066312">DnaA protein, Bacteria</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029968">Escherichia coli Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>138861-88-8</RegistryNumber><NameOfSubstance UI="C068863">argP protein, E coli</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002876" MajorTopicYN="N">Chromosomes, Bacterial</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004261" MajorTopicYN="Y">DNA Replication</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004269" MajorTopicYN="N">DNA, Bacterial</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004268" MajorTopicYN="N">DNA-Binding Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029968" MajorTopicYN="Y">Escherichia coli Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010957" MajorTopicYN="N">Plasmids</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1992</Year><Month>2</Month><Day>5</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1992</Year><Month>2</Month><Day>5</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1992</Year><Month>2</Month><Day>5</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">1733927</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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