DNA Replication Fork Arrest by the Bacillus subtilis RTP-DNA Complex Involves a Mechanism that Is Independent of the Affinity of RTP-DNA Binding

G. Duggin, I

DNA Replication Fork Arrest by the Bacillus subtilis RTP-DNA Complex Involves a Mechanism that Is Independent of the Affinity of RTP-DNA Binding

G. Duggin, I

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Publication Type:: Journal Article
Citation:: Journal of Molecular Biology, 2006, 361 (1), pp. 1 - 6
Issue Date:: 2006-08-04

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Field	Value	Language
dc.contributor.author	G. Duggin, I https://orcid.org/0000-0003-4868-7350	en_US
dc.date.available	2006-06-05	en_US
dc.date.issued	2006-08-04	en_US
dc.identifier.citation	Journal of Molecular Biology, 2006, 361 (1), pp. 1 - 6	en_US
dc.identifier.issn	0022-2836	en_US
dc.identifier.uri	http://hdl.handle.net/10453/14791
dc.description.abstract	In order to elucidate the mechanism of DNA replication fork arrest by the replication terminator protein (RTP)-DNA complex, a set of RTP fusion proteins were constructed in which peptides of various sizes were fused to the C terminus; this placed the peptides at a surface location that was predicted to come into contact with the DNA replication machinery during fork arrest. The fusion proteins were capable of replication fork arrest in vivo, but they had a significantly reduced efficiency compared to wild-type RTP, which was not directly proportional to peptide size or sequence. Importantly, the fusion proteins retained completely normal RTP-DNA binding affinity. These findings rule out the molecular clamp model as the sole explanation for fork arrest by RTP, and suggest that RTP interacts with the replication machinery in a manner that directly contributes to the fork arrest mechanism. Crown Copyright © 2006.	en_US
dc.relation.ispartof	Journal of Molecular Biology	en_US
dc.relation.isbasedon	10.1016/j.jmb.2006.06.013	en_US
dc.subject.classification	Biochemistry & Molecular Biology	en_US
dc.subject.mesh	Bacillus subtilis	en_US
dc.subject.mesh	Bacterial Proteins	en_US
dc.subject.mesh	DNA-Binding Proteins	en_US
dc.subject.mesh	DNA, Bacterial	en_US
dc.subject.mesh	DNA Replication	en_US
dc.subject.mesh	Protein Binding	en_US
dc.title	DNA Replication Fork Arrest by the Bacillus subtilis RTP-DNA Complex Involves a Mechanism that Is Independent of the Affinity of RTP-DNA Binding	en_US
dc.type	Journal Article
utslib.citation.volume	1	en_US
utslib.citation.volume	361	en_US
utslib.for	0601 Biochemistry and Cell Biology	en_US
utslib.for	0304 Medicinal and Biomolecular Chemistry	en_US
utslib.for	0605 Microbiology	en_US
dc.location.activity	Chongqing, China
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - ithree - Institute of Infection, Immunity and Innovation
utslib.copyright.status	closed_access
pubs.issue	1	en_US
pubs.publication-status	Published	en_US
pubs.volume	361	en_US

Abstract:

In order to elucidate the mechanism of DNA replication fork arrest by the replication terminator protein (RTP)-DNA complex, a set of RTP fusion proteins were constructed in which peptides of various sizes were fused to the C terminus; this placed the peptides at a surface location that was predicted to come into contact with the DNA replication machinery during fork arrest. The fusion proteins were capable of replication fork arrest in vivo, but they had a significantly reduced efficiency compared to wild-type RTP, which was not directly proportional to peptide size or sequence. Importantly, the fusion proteins retained completely normal RTP-DNA binding affinity. These findings rule out the molecular clamp model as the sole explanation for fork arrest by RTP, and suggest that RTP interacts with the replication machinery in a manner that directly contributes to the fork arrest mechanism. Crown Copyright © 2006.

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http://hdl.handle.net/10453/14791