The Plasmid RK2 Replication Initiator Protein (TrfA) Binds to the Sliding Clamp β Subunit of DNA Polymerase III: Implication for the Toxicity of a Peptide Derived from the Amino-Terminal Portion of 33-Kilodalton TrfA
Identifieur interne : 000204 ( Ncbi/Curation ); précédent : 000203; suivant : 000205The Plasmid RK2 Replication Initiator Protein (TrfA) Binds to the Sliding Clamp β Subunit of DNA Polymerase III: Implication for the Toxicity of a Peptide Derived from the Amino-Terminal Portion of 33-Kilodalton TrfA
Auteurs : Kritaya Kongsuwan ; Peter Josh ; Marc J. Picault ; Gene Wijffels ; Brian DalrympleSource :
- Journal of Bacteriology [ 0021-9193 ] ; 2006.
Abstract
The broad-host-range plasmid RK2 is capable of replication and stable maintenance within a wide range of gram-negative bacterial hosts. It encodes the essential replication initiation protein TrfA, which binds to the host initiation protein, DnaA, at the plasmid origin of replication (
Url:
DOI: 10.1128/JB.00231-06
PubMed: 16855240
PubMed Central: 1540049
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The Plasmid RK2 Replication Initiator Protein (TrfA) Binds to the Sliding Clamp β Subunit of DNA Polymerase III: Implication for the Toxicity of a Peptide Derived from the Amino-Terminal Portion of 33-Kilodalton TrfA</title><author><name sortKey="Kongsuwan, Kritaya" sort="Kongsuwan, Kritaya" uniqKey="Kongsuwan K" first="Kritaya" last="Kongsuwan">Kritaya Kongsuwan</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Josh, Peter" sort="Josh, Peter" uniqKey="Josh P" first="Peter" last="Josh">Peter Josh</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Picault, Marc J" sort="Picault, Marc J" uniqKey="Picault M" first="Marc J." last="Picault">Marc J. Picault</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Wijffels, Gene" sort="Wijffels, Gene" uniqKey="Wijffels G" first="Gene" last="Wijffels">Gene Wijffels</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Dalrymple, Brian" sort="Dalrymple, Brian" uniqKey="Dalrymple B" first="Brian" last="Dalrymple">Brian Dalrymple</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">16855240</idno><idno type="pmc">1540049</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1540049</idno><idno type="RBID">PMC:1540049</idno><idno type="doi">10.1128/JB.00231-06</idno><date when="2006">2006</date><idno type="wicri:Area/Pmc/Corpus">001006</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001006</idno><idno type="wicri:Area/Pmc/Curation">000E67</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000E67</idno><idno type="wicri:Area/Pmc/Checkpoint">002B76</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">002B76</idno><idno type="wicri:Area/Ncbi/Merge">000204</idno><idno type="wicri:Area/Ncbi/Curation">000204</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">The Plasmid RK2 Replication Initiator Protein (TrfA) Binds to the Sliding Clamp β Subunit of DNA Polymerase III: Implication for the Toxicity of a Peptide Derived from the Amino-Terminal Portion of 33-Kilodalton TrfA</title><author><name sortKey="Kongsuwan, Kritaya" sort="Kongsuwan, Kritaya" uniqKey="Kongsuwan K" first="Kritaya" last="Kongsuwan">Kritaya Kongsuwan</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Josh, Peter" sort="Josh, Peter" uniqKey="Josh P" first="Peter" last="Josh">Peter Josh</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Picault, Marc J" sort="Picault, Marc J" uniqKey="Picault M" first="Marc J." last="Picault">Marc J. Picault</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Wijffels, Gene" sort="Wijffels, Gene" uniqKey="Wijffels G" first="Gene" last="Wijffels">Gene Wijffels</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Dalrymple, Brian" sort="Dalrymple, Brian" uniqKey="Dalrymple B" first="Brian" last="Dalrymple">Brian Dalrymple</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author></analytic><series><title level="j">Journal of Bacteriology</title><idno type="ISSN">0021-9193</idno><idno type="eISSN">1098-5530</idno><imprint><date when="2006">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The broad-host-range plasmid RK2 is capable of replication and stable maintenance within a wide range of gram-negative bacterial hosts. It encodes the essential replication initiation protein TrfA, which binds to the host initiation protein, DnaA, at the plasmid origin of replication (<italic>oriV</italic>). There are two versions of the TrfA protein, 44 and 33 kDa, resulting from alternate in-frame translational starts. We have shown that the smaller protein, TrfA-33, and its 64-residue amino-terminal peptide (designated T1) physically interact with the <italic>Escherichia coli</italic> β sliding clamp (β<sub>2</sub>). This interaction appears to be mediated through a QLSLF peptide motif located near the amino-terminal end of TrfA-33 and T1, which is identical to the previously described eubacterial clamp-binding consensus motif. T1 forms a stable complex with β<sub>2</sub> and was found to inhibit plasmid RK2 replication in vitro. This specific interaction between T1 and β<sub>2</sub> and the ability of T1 to block DNA replication have implications for the previously reported cell lethality caused by overproduction of T1 (P. D. Kim, T. M. Rosche, and W. Firshein, Plasmid 43:214-222, 2000). The toxicity of T1 was suppressed when wild-type T1 was replaced with mutant T1, carrying an LF deletion in the β-binding motif. Previously, T1 toxicity has been shown to be suppressed by Hda, an intermediate regulatory protein which helps prevent overinitiation in <italic>E. coli</italic> through its interaction with the initiator protein, DnaA, and β<sub>2</sub>. Our results support a model in which T1 toxicity is caused by T1 binding to β<sub>2</sub>, especially when T1 is overexpressed, preventing β<sub>2</sub> from interacting with host replication proteins such as Hda during the early events of chromosome replication.</p></div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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