AustralieFrV1, Main, Exploration, bibRecordById, PMC:1540049

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 : 009B51 ( Main/Exploration ); précédent : 009B50; suivant : 009B52

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

Auteurs : Kritaya Kongsuwan [Australie] ; Peter Josh [Australie] ; Marc J. Picault [France] ; Gene Wijffels [Australie] ; Brian Dalrymple [Australie]

Source :

Journal of bacteriology [ 0021-9193 ] ; 2006.

RBID : Pascal:06-0382062

Descripteurs français

Pascal (Inist)
- Plasmide, Réplication, Protéine, DNA-directed DNA polymerase, Sousunité, Toxicité, Peptide, Microbiologie, Bactériologie.

English descriptors

KwdEn :
- Bacteriology, DNA-directed DNA polymerase, Microbiology, Peptides, Plasmid, Protein, Replication, Subunit, Toxicity.

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 (oriV). 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 Escherichia coli β sliding clamp (β₂). 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 β₂ and was found to inhibit plasmid RK2 replication in vitro. This specific interaction between T1 and β₂ and the ability of Tl 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 E. coli through its interaction with the initiator protein, DnaA, and β₂. Our results support a model in which T1 toxicity is caused by T1 binding to β₂, especially when T1 is overexpressed, preventing β₂ from interacting with host replication proteins such as Hda during the early events of chromosome replication.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1540049

Affiliations:

Australie, France

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<front><div type="abstract" xml:lang="en">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 (oriV). 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 Escherichia coli 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 Tl 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 E. coli 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.</div>
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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

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

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

	Serveur d'exploration sur les relations entre la France et l'Australie
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