The dnaA initiator protein binds separate domains in the replication origin of Escherichia coli.
Identifieur interne : 004A92 ( Main/Exploration ); précédent : 004A91; suivant : 004A93The dnaA initiator protein binds separate domains in the replication origin of Escherichia coli.
Auteurs : B Y Yung [États-Unis] ; A. KornbergSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1989.
Descripteurs français
- KwdFr :
- ADN bactérien (métabolisme), ADN superhélicoïdal (métabolisme), ADP (métabolisme), Adénosine triphosphate (métabolisme), Escherichia coli (métabolisme), Fixation compétitive, Fragments peptidiques (métabolisme), Plasmides, Protéines bactériennes (métabolisme), Protéines de liaison à l'ADN (métabolisme), Relation structure-activité, Réplication de l'ADN, Séquences d'acides nucléiques régulatrices, Température, Trypsine (pharmacologie).
- MESH :
- métabolisme : ADN bactérien, ADN superhélicoïdal, ADP, Adénosine triphosphate, Escherichia coli, Fragments peptidiques, Protéines bactériennes, Protéines de liaison à l'ADN.
- pharmacologie : Trypsine.
- Fixation compétitive, Plasmides, Relation structure-activité, Réplication de l'ADN, Séquences d'acides nucléiques régulatrices, Température.
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
Affiliations:
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Le document en format XML
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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><idno type="wicri:Area/PubMed/Curation">002A42</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002A42</idno><idno type="wicri:Area/PubMed/Checkpoint">002878</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002878</idno><idno type="wicri:Area/Ncbi/Merge">000F56</idno><idno type="wicri:Area/Ncbi/Curation">000F56</idno><idno type="wicri:Area/Ncbi/Checkpoint">000F56</idno><idno type="wicri:doubleKey">0021-9258:1989:Yung B:the:dnaa:initiator</idno><idno type="wicri:Area/Main/Merge">004B70</idno><idno type="wicri:Area/Main/Curation">004A92</idno><idno type="wicri:Area/Main/Exploration">004A92</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 wicri:level="2"><nlm:affiliation>Department of Biochemistry, Stanford University School of Medicine, California 94305-5307.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Department of Biochemistry, Stanford University School of Medicine</wicri:cityArea></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="KwdFr" xml:lang="fr"><term>ADN bactérien (métabolisme)</term><term>ADN superhélicoïdal (métabolisme)</term><term>ADP (métabolisme)</term><term>Adénosine triphosphate (métabolisme)</term><term>Escherichia coli (métabolisme)</term><term>Fixation compétitive</term><term>Fragments peptidiques (métabolisme)</term><term>Plasmides</term><term>Protéines bactériennes (métabolisme)</term><term>Protéines de liaison à l'ADN (métabolisme)</term><term>Relation structure-activité</term><term>Réplication de l'ADN</term><term>Séquences d'acides nucléiques régulatrices</term><term>Température</term><term>Trypsine (pharmacologie)</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" qualifier="métabolisme" xml:lang="fr"><term>ADN bactérien</term><term>ADN superhélicoïdal</term><term>ADP</term><term>Adénosine triphosphate</term><term>Escherichia coli</term><term>Fragments peptidiques</term><term>Protéines bactériennes</term><term>Protéines de liaison à l'ADN</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Trypsine</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><keywords scheme="MESH" xml:lang="fr"><term>Fixation compétitive</term><term>Plasmides</term><term>Relation structure-activité</term><term>Réplication de l'ADN</term><term>Séquences d'acides nucléiques régulatrices</term><term>Température</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><affiliations><list><country><li>États-Unis</li></country><region><li>Californie</li></region></list><tree><noCountry><name sortKey="Kornberg, A" sort="Kornberg, A" uniqKey="Kornberg A" first="A" last="Kornberg">A. Kornberg</name></noCountry><country name="États-Unis"><region name="Californie"><name sortKey="Yung, B Y" sort="Yung, B Y" uniqKey="Yung B" first="B Y" last="Yung">B Y Yung</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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