The dnaA initiator protein binds separate domains in the replication origin of Escherichia coli.
Identifieur interne : 002A42 ( PubMed/Corpus ); précédent : 002A41; suivant : 002A43The dnaA initiator protein binds separate domains in the replication origin of Escherichia coli.
Auteurs : B Y Yung ; A. KornbergSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1989.
English descriptors
- KwdEn :
- Adenosine Diphosphate (metabolism), Adenosine Triphosphate (metabolism), Bacterial Proteins (metabolism), Binding, Competitive, DNA Replication, DNA, Bacterial (metabolism), DNA, Superhelical (metabolism), DNA-Binding Proteins (metabolism), Escherichia coli (metabolism), Peptide Fragments (metabolism), Plasmids, Regulatory Sequences, Nucleic Acid, Structure-Activity Relationship, Temperature, Trypsin (pharmacology).
- MESH :
- chemical , metabolism : Adenosine Diphosphate, Adenosine Triphosphate, Bacterial Proteins, DNA, Bacterial, DNA, Superhelical, DNA-Binding Proteins, Peptide Fragments.
- metabolism : Escherichia coli.
- chemical , pharmacology : Trypsin.
- Binding, Competitive, DNA Replication, Plasmids, Regulatory Sequences, Nucleic Acid, Structure-Activity Relationship, Temperature.
Abstract
After binding to its four 9-mer boxes in the 245-base pair Escherichia coli replication origin (oriC), dnaA protein effects the formation of an "open complex" in an adjacent region made up of three 13-mers (Bramhill, D., and Kornberg, A. (1988) Cell 52, 743-755). This open complex formation requires the ATP form of dnaA protein assisted by HU protein (Sekimizu, K., Bramhill, D., and Kornberg, A. (1987) Cell 50, 259-265). We now provide direct evidence that dnaA protein binds the 13-mers, sequences that bear no resemblance to the 9-mer box. The evidence is (i) displacement of dnaA protein from the open complex by oriC or by a synthetic oligonucleotide containing the 13-mers, but not by a mutant of oriC lacking the 13-mers; (ii) filter binding of the synthetic (13-mer) oligonucleotide by dnaA protein; and (iii) requirement for the ATP form of dnaA protein assisted by HU protein for temperature-dependent binding to the 13-mer region. Controlled proteolysis of dnaA protein results in a prompt loss of oriC binding; an NH2-terminal 30-kDa peptide contains the domain that binds ATP and phospholipids known to destabilize the tightly bound ATP.
PubMed: 2539372
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Kornberg</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1989">1989</date><idno type="RBID">pubmed:2539372</idno><idno type="pmid">2539372</idno><idno type="wicri:Area/PubMed/Corpus">002A42</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002A42</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The dnaA initiator protein binds separate domains in the replication origin of Escherichia coli.</title><author><name sortKey="Yung, B Y" sort="Yung, B Y" uniqKey="Yung B" first="B Y" last="Yung">B Y Yung</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></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="1989" type="published">1989</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adenosine Diphosphate (metabolism)</term><term>Adenosine Triphosphate (metabolism)</term><term>Bacterial Proteins (metabolism)</term><term>Binding, Competitive</term><term>DNA Replication</term><term>DNA, Bacterial (metabolism)</term><term>DNA, Superhelical (metabolism)</term><term>DNA-Binding Proteins (metabolism)</term><term>Escherichia coli (metabolism)</term><term>Peptide Fragments (metabolism)</term><term>Plasmids</term><term>Regulatory Sequences, Nucleic Acid</term><term>Structure-Activity Relationship</term><term>Temperature</term><term>Trypsin (pharmacology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adenosine Diphosphate</term><term>Adenosine Triphosphate</term><term>Bacterial Proteins</term><term>DNA, Bacterial</term><term>DNA, Superhelical</term><term>DNA-Binding Proteins</term><term>Peptide Fragments</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Trypsin</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding, Competitive</term><term>DNA Replication</term><term>Plasmids</term><term>Regulatory Sequences, Nucleic Acid</term><term>Structure-Activity Relationship</term><term>Temperature</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">After binding to its four 9-mer boxes in the 245-base pair Escherichia coli replication origin (oriC), dnaA protein effects the formation of an "open complex" in an adjacent region made up of three 13-mers (Bramhill, D., and Kornberg, A. (1988) Cell 52, 743-755). This open complex formation requires the ATP form of dnaA protein assisted by HU protein (Sekimizu, K., Bramhill, D., and Kornberg, A. (1987) Cell 50, 259-265). We now provide direct evidence that dnaA protein binds the 13-mers, sequences that bear no resemblance to the 9-mer box. The evidence is (i) displacement of dnaA protein from the open complex by oriC or by a synthetic oligonucleotide containing the 13-mers, but not by a mutant of oriC lacking the 13-mers; (ii) filter binding of the synthetic (13-mer) oligonucleotide by dnaA protein; and (iii) requirement for the ATP form of dnaA protein assisted by HU protein for temperature-dependent binding to the 13-mer region. Controlled proteolysis of dnaA protein results in a prompt loss of oriC binding; an NH2-terminal 30-kDa peptide contains the domain that binds ATP and phospholipids known to destabilize the tightly bound ATP.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">2539372</PMID><DateCompleted><Year>1989</Year><Month>05</Month><Day>18</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>264</Volume><Issue>11</Issue><PubDate><Year>1989</Year><Month>Apr</Month><Day>15</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J. Biol. Chem.</ISOAbbreviation></Journal><ArticleTitle>The dnaA initiator protein binds separate domains in the replication origin of Escherichia coli.</ArticleTitle><Pagination><MedlinePgn>6146-50</MedlinePgn></Pagination><Abstract><AbstractText>After binding to its four 9-mer boxes in the 245-base pair Escherichia coli replication origin (oriC), dnaA protein effects the formation of an "open complex" in an adjacent region made up of three 13-mers (Bramhill, D., and Kornberg, A. (1988) Cell 52, 743-755). This open complex formation requires the ATP form of dnaA protein assisted by HU protein (Sekimizu, K., Bramhill, D., and Kornberg, A. (1987) Cell 50, 259-265). We now provide direct evidence that dnaA protein binds the 13-mers, sequences that bear no resemblance to the 9-mer box. The evidence is (i) displacement of dnaA protein from the open complex by oriC or by a synthetic oligonucleotide containing the 13-mers, but not by a mutant of oriC lacking the 13-mers; (ii) filter binding of the synthetic (13-mer) oligonucleotide by dnaA protein; and (iii) requirement for the ATP form of dnaA protein assisted by HU protein for temperature-dependent binding to the 13-mer region. Controlled proteolysis of dnaA protein results in a prompt loss of oriC binding; an NH2-terminal 30-kDa peptide contains the domain that binds ATP and phospholipids known to destabilize the tightly bound ATP.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yung</LastName><ForeName>B Y</ForeName><Initials>BY</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Stanford University School of Medicine, California 94305-5307.</Affiliation></AffiliationInfo></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="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="D004278">DNA, Superhelical</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004268">DNA-Binding Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010446">Peptide Fragments</NameOfSubstance></Chemical><Chemical><RegistryNumber>61D2G4IYVH</RegistryNumber><NameOfSubstance UI="D000244">Adenosine Diphosphate</NameOfSubstance></Chemical><Chemical><RegistryNumber>8L70Q75FXE</RegistryNumber><NameOfSubstance UI="D000255">Adenosine 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Replication</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004269" MajorTopicYN="N">DNA, Bacterial</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004278" MajorTopicYN="N">DNA, Superhelical</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004268" MajorTopicYN="N">DNA-Binding Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010446" MajorTopicYN="N">Peptide Fragments</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010957" 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PubStatus="entrez"><Year>1989</Year><Month>4</Month><Day>15</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">2539372</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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