Interaction of SeqA and Dam methylase on the hemimethylated origin of Escherichia coli chromosomal DNA replication.
Identifieur interne : 003803 ( Main/Exploration ); précédent : 003802; suivant : 003804Interaction of SeqA and Dam methylase on the hemimethylated origin of Escherichia coli chromosomal DNA replication.
Auteurs : S. Kang [Corée du Sud] ; H. Lee ; J S Han ; D S HwangSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1999.
Descripteurs français
- KwdFr :
- ADN bactérien, Chromosomes de bactérie, Données de séquences moléculaires, Escherichia coli (génétique), Facteurs de transcription, Liaison aux protéines, Méthylation de l'ADN, Origine de réplication, Protéines Escherichia coli, Protéines bactériennes (métabolisme), Protéines de la membrane externe bactérienne, Protéines de liaison à l'ADN, Site-specific DNA-methyltransferase (adenine-specific) (métabolisme), Séquence nucléotidique.
- MESH :
- génétique : Escherichia coli.
- métabolisme : Protéines bactériennes, Site-specific DNA-methyltransferase (adenine-specific).
- ADN bactérien, Chromosomes de bactérie, Données de séquences moléculaires, Facteurs de transcription, Liaison aux protéines, Méthylation de l'ADN, Origine de réplication, Protéines Escherichia coli, Protéines de la membrane externe bactérienne, Protéines de liaison à l'ADN, Séquence nucléotidique.
English descriptors
- KwdEn :
- Bacterial Outer Membrane Proteins, Bacterial Proteins (metabolism), Base Sequence, Chromosomes, Bacterial, DNA Methylation, DNA, Bacterial, DNA-Binding Proteins, Escherichia coli (genetics), Escherichia coli Proteins, Molecular Sequence Data, Protein Binding, Replication Origin, Site-Specific DNA-Methyltransferase (Adenine-Specific) (metabolism), Transcription Factors.
- MESH :
- chemical , metabolism : Bacterial Proteins, Site-Specific DNA-Methyltransferase (Adenine-Specific).
- chemical : Bacterial Outer Membrane Proteins, DNA, Bacterial, DNA-Binding Proteins, Escherichia coli Proteins, Transcription Factors.
- genetics : Escherichia coli.
- Base Sequence, Chromosomes, Bacterial, DNA Methylation, Molecular Sequence Data, Protein Binding, Replication Origin.
Abstract
Preferential binding of SeqA protein to hemimethylated oriC, the origin of Escherichia coli chromosomal replication, delays methylation by Dam methylase. Because the SeqA-oriC interaction appears to be essential in timing of chromosomal replication initiation, the biochemical functions of SeqA protein and Dam methylase at the 13-mer L, M, and R region containing 4 GATC sequences at the left end of oriC were examined. We found that SeqA protein preferentially bound hemimethylated 13-mers but not fully nor unmethylated 13-mers. Regardless of strand methylation, the binding of SeqA protein to the hemimethylated GATC sequence of 13-mer L was followed by additional binding to other hemimethylated GATC sequences of 13-mer M and R. On the other hand, Dam methylase did not discriminate binding of 13-mers in different methylation patterns and was not specific to GATC sequences. The binding specificity and higher affinity of SeqA protein over Dam methylase to the hemimethylated 13-mers along with the reported cellular abundance of this protein explains the dominant action of SeqA protein over Dam methylase to the newly replicated oriC for the sequestration of chromosomal replication. Furthermore, SeqA protein bound to hemimethylated 13-mers was not dissociated by Dam methylase, and most SeqA protein spontaneously dissociated 10 min after binding. Also, SeqA protein delayed the in vitro methylation of hemimethylated 13-mers by Dam methylase. These in vitro results suggest that the intrinsic binding instability of SeqA protein results in release of sequestrated hemimethylated oriC.
DOI: 10.1074/jbc.274.17.11463
PubMed: 10206949
Affiliations:
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Lee</name></author><author><name sortKey="Han, J S" sort="Han, J S" uniqKey="Han J" first="J S" last="Han">J S Han</name></author><author><name sortKey="Hwang, D S" sort="Hwang, D S" uniqKey="Hwang D" first="D S" last="Hwang">D S Hwang</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1999">1999</date><idno type="RBID">pubmed:10206949</idno><idno type="pmid">10206949</idno><idno type="doi">10.1074/jbc.274.17.11463</idno><idno type="wicri:Area/PubMed/Corpus">002634</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002634</idno><idno type="wicri:Area/PubMed/Curation">002634</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002634</idno><idno type="wicri:Area/PubMed/Checkpoint">002491</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002491</idno><idno type="wicri:Area/Ncbi/Merge">000014</idno><idno type="wicri:Area/Ncbi/Curation">000014</idno><idno type="wicri:Area/Ncbi/Checkpoint">000014</idno><idno type="wicri:doubleKey">0021-9258:1999:Kang S:interaction:of:seqa</idno><idno type="wicri:Area/Main/Merge">003847</idno><idno type="wicri:Area/Main/Curation">003803</idno><idno type="wicri:Area/Main/Exploration">003803</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Interaction of SeqA and Dam methylase on the hemimethylated origin of Escherichia coli chromosomal DNA replication.</title><author><name sortKey="Kang, S" sort="Kang, S" uniqKey="Kang S" first="S" last="Kang">S. Kang</name><affiliation wicri:level="4"><nlm:affiliation>Institute for Molecular Biology and Genetics, Seoul National University, Seoul 151-742, Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>Institute for Molecular Biology and Genetics, Seoul National University, Seoul 151-742</wicri:regionArea><placeName><settlement type="city">Séoul</settlement><region type="capital">Région capitale de Séoul</region></placeName><orgName type="university">Université nationale de Séoul</orgName><placeName><settlement type="city">Séoul</settlement></placeName></affiliation></author><author><name sortKey="Lee, H" sort="Lee, H" uniqKey="Lee H" first="H" last="Lee">H. Lee</name></author><author><name sortKey="Han, J S" sort="Han, J S" uniqKey="Han J" first="J S" last="Han">J S Han</name></author><author><name sortKey="Hwang, D S" sort="Hwang, D S" uniqKey="Hwang D" first="D S" last="Hwang">D S Hwang</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="1999" type="published">1999</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacterial Outer Membrane Proteins</term><term>Bacterial Proteins (metabolism)</term><term>Base Sequence</term><term>Chromosomes, Bacterial</term><term>DNA Methylation</term><term>DNA, Bacterial</term><term>DNA-Binding Proteins</term><term>Escherichia coli (genetics)</term><term>Escherichia coli Proteins</term><term>Molecular Sequence Data</term><term>Protein Binding</term><term>Replication Origin</term><term>Site-Specific DNA-Methyltransferase (Adenine-Specific) (metabolism)</term><term>Transcription Factors</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN bactérien</term><term>Chromosomes de bactérie</term><term>Données de séquences moléculaires</term><term>Escherichia coli (génétique)</term><term>Facteurs de transcription</term><term>Liaison aux protéines</term><term>Méthylation de l'ADN</term><term>Origine de réplication</term><term>Protéines Escherichia coli</term><term>Protéines bactériennes (métabolisme)</term><term>Protéines de la membrane externe bactérienne</term><term>Protéines de liaison à l'ADN</term><term>Site-specific DNA-methyltransferase (adenine-specific) (métabolisme)</term><term>Séquence nucléotidique</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Bacterial Proteins</term><term>Site-Specific DNA-Methyltransferase (Adenine-Specific)</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Bacterial Outer Membrane Proteins</term><term>DNA, Bacterial</term><term>DNA-Binding Proteins</term><term>Escherichia coli Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines bactériennes</term><term>Site-specific DNA-methyltransferase (adenine-specific)</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Base Sequence</term><term>Chromosomes, Bacterial</term><term>DNA Methylation</term><term>Molecular Sequence Data</term><term>Protein Binding</term><term>Replication Origin</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>ADN bactérien</term><term>Chromosomes de bactérie</term><term>Données de séquences moléculaires</term><term>Facteurs de transcription</term><term>Liaison aux protéines</term><term>Méthylation de l'ADN</term><term>Origine de réplication</term><term>Protéines Escherichia coli</term><term>Protéines de la membrane externe bactérienne</term><term>Protéines de liaison à l'ADN</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Preferential binding of SeqA protein to hemimethylated oriC, the origin of Escherichia coli chromosomal replication, delays methylation by Dam methylase. Because the SeqA-oriC interaction appears to be essential in timing of chromosomal replication initiation, the biochemical functions of SeqA protein and Dam methylase at the 13-mer L, M, and R region containing 4 GATC sequences at the left end of oriC were examined. We found that SeqA protein preferentially bound hemimethylated 13-mers but not fully nor unmethylated 13-mers. Regardless of strand methylation, the binding of SeqA protein to the hemimethylated GATC sequence of 13-mer L was followed by additional binding to other hemimethylated GATC sequences of 13-mer M and R. On the other hand, Dam methylase did not discriminate binding of 13-mers in different methylation patterns and was not specific to GATC sequences. The binding specificity and higher affinity of SeqA protein over Dam methylase to the hemimethylated 13-mers along with the reported cellular abundance of this protein explains the dominant action of SeqA protein over Dam methylase to the newly replicated oriC for the sequestration of chromosomal replication. Furthermore, SeqA protein bound to hemimethylated 13-mers was not dissociated by Dam methylase, and most SeqA protein spontaneously dissociated 10 min after binding. Also, SeqA protein delayed the in vitro methylation of hemimethylated 13-mers by Dam methylase. These in vitro results suggest that the intrinsic binding instability of SeqA protein results in release of sequestrated hemimethylated oriC.</div></front></TEI><affiliations><list><country><li>Corée du Sud</li></country><region><li>Région capitale de Séoul</li></region><settlement><li>Séoul</li></settlement><orgName><li>Université nationale de Séoul</li></orgName></list><tree><noCountry><name sortKey="Han, J S" sort="Han, J S" uniqKey="Han J" first="J S" last="Han">J S Han</name><name sortKey="Hwang, D S" sort="Hwang, D S" uniqKey="Hwang D" first="D S" last="Hwang">D S Hwang</name><name sortKey="Lee, H" sort="Lee, H" uniqKey="Lee H" first="H" last="Lee">H. Lee</name></noCountry><country name="Corée du Sud"><region name="Région capitale de Séoul"><name sortKey="Kang, S" sort="Kang, S" uniqKey="Kang S" first="S" last="Kang">S. Kang</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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