A novel protein binds a key origin sequence to block replication of an E. coli minichromosome.
Identifieur interne : 002A19 ( PubMed/Corpus ); précédent : 002A18; suivant : 002A20A novel protein binds a key origin sequence to block replication of an E. coli minichromosome.
Auteurs : D S Hwang ; A. KornbergSource :
- Cell [ 0092-8674 ] ; 1990.
English descriptors
- KwdEn :
- Base Sequence, Chromatography, Affinity, Chromatography, Ion Exchange, Chromosomes, Bacterial, DNA Replication, DNA, Bacterial (genetics), DNA-Binding Proteins (isolation & purification), DNA-Binding Proteins (metabolism), Deoxyribonuclease I, Escherichia coli (genetics), Escherichia coli (metabolism), Kinetics, Molecular Sequence Data, Molecular Weight, Oligonucleotide Probes, Plasmids, Restriction Mapping.
- MESH :
- chemical , genetics : DNA, Bacterial.
- chemical , isolation & purification : DNA-Binding Proteins.
- chemical , metabolism : DNA-Binding Proteins.
- genetics : Escherichia coli.
- metabolism : Escherichia coli.
- Base Sequence, Chromatography, Affinity, Chromatography, Ion Exchange, Chromosomes, Bacterial, DNA Replication, Deoxyribonuclease I, Kinetics, Molecular Sequence Data, Molecular Weight, Oligonucleotide Probes, Plasmids, Restriction Mapping.
Abstract
A sequence of three tandem repeats of a 13-mer in the replication origin (oriC) of E. coli is the highly conserved site of opening of the duplex for initiation of DNA synthesis. A protein that binds this sequence has been discovered in E. coli and purified to homogeneity. This novel 33 kd polypeptide behaves as a dimer. Binding to the 13-mers is specific and limited to this region. At a ratio of 10-20 monomers per oriC plasmid, the binding blocks initiation by preventing the opening of the 13-mer region by dnaA protein. Once the 13-mers are opened by dnaA protein action, the 33 kd protein is without effect on the subsequent stages of replication. The specificity of binding and profound inhibitory effect suggest a regulatory role for this protein at an early stage of chromosome initiation.
DOI: 10.1016/0092-8674(90)90165-b
PubMed: 2208289
Links to Exploration step
pubmed:2208289Le document en format XML
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<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="Kornberg, A" sort="Kornberg, A" uniqKey="Kornberg A" first="A" last="Kornberg">A. Kornberg</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">A novel protein binds a key origin sequence to block replication of an E. coli minichromosome.</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>
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<author><name sortKey="Kornberg, A" sort="Kornberg, A" uniqKey="Kornberg A" first="A" last="Kornberg">A. Kornberg</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Base Sequence</term>
<term>Chromatography, Affinity</term>
<term>Chromatography, Ion Exchange</term>
<term>Chromosomes, Bacterial</term>
<term>DNA Replication</term>
<term>DNA, Bacterial (genetics)</term>
<term>DNA-Binding Proteins (isolation & purification)</term>
<term>DNA-Binding Proteins (metabolism)</term>
<term>Deoxyribonuclease I</term>
<term>Escherichia coli (genetics)</term>
<term>Escherichia coli (metabolism)</term>
<term>Kinetics</term>
<term>Molecular Sequence Data</term>
<term>Molecular Weight</term>
<term>Oligonucleotide Probes</term>
<term>Plasmids</term>
<term>Restriction Mapping</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA, Bacterial</term>
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<keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>DNA-Binding Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>DNA-Binding Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term>
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<keywords scheme="MESH" xml:lang="en"><term>Base Sequence</term>
<term>Chromatography, Affinity</term>
<term>Chromatography, Ion Exchange</term>
<term>Chromosomes, Bacterial</term>
<term>DNA Replication</term>
<term>Deoxyribonuclease I</term>
<term>Kinetics</term>
<term>Molecular Sequence Data</term>
<term>Molecular Weight</term>
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<front><div type="abstract" xml:lang="en">A sequence of three tandem repeats of a 13-mer in the replication origin (oriC) of E. coli is the highly conserved site of opening of the duplex for initiation of DNA synthesis. A protein that binds this sequence has been discovered in E. coli and purified to homogeneity. This novel 33 kd polypeptide behaves as a dimer. Binding to the 13-mers is specific and limited to this region. At a ratio of 10-20 monomers per oriC plasmid, the binding blocks initiation by preventing the opening of the 13-mer region by dnaA protein. Once the 13-mers are opened by dnaA protein action, the 33 kd protein is without effect on the subsequent stages of replication. The specificity of binding and profound inhibitory effect suggest a regulatory role for this protein at an early stage of chromosome initiation.</div>
</front>
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<DateCompleted><Year>1990</Year>
<Month>11</Month>
<Day>19</Day>
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<DateRevised><Year>2019</Year>
<Month>07</Month>
<Day>05</Day>
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<Article PubModel="Print"><Journal><ISSN IssnType="Print">0092-8674</ISSN>
<JournalIssue CitedMedium="Print"><Volume>63</Volume>
<Issue>2</Issue>
<PubDate><Year>1990</Year>
<Month>Oct</Month>
<Day>19</Day>
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<Title>Cell</Title>
<ISOAbbreviation>Cell</ISOAbbreviation>
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<ArticleTitle>A novel protein binds a key origin sequence to block replication of an E. coli minichromosome.</ArticleTitle>
<Pagination><MedlinePgn>325-31</MedlinePgn>
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<Abstract><AbstractText>A sequence of three tandem repeats of a 13-mer in the replication origin (oriC) of E. coli is the highly conserved site of opening of the duplex for initiation of DNA synthesis. A protein that binds this sequence has been discovered in E. coli and purified to homogeneity. This novel 33 kd polypeptide behaves as a dimer. Binding to the 13-mers is specific and limited to this region. At a ratio of 10-20 monomers per oriC plasmid, the binding blocks initiation by preventing the opening of the 13-mer region by dnaA protein. Once the 13-mers are opened by dnaA protein action, the 33 kd protein is without effect on the subsequent stages of replication. The specificity of binding and profound inhibitory effect suggest a regulatory role for this protein at an early stage of chromosome initiation.</AbstractText>
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