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Escherichia coli Rep DNA helicase and error-prone DNA polymerase IV interact physically and functionally.
Mol Microbiol. 2011 Apr; 80(2):524-41
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20 May 2011
Martin Marinus
F1000 Microbiology
University of Massachusetts Medical School,
Worcester, Massachusetts, USA.
F1000 Microbiology
University of Massachusetts Medical School,
Worcester, Massachusetts, USA.
New Finding
DOI: 10.3410/f.10652959.11531057
This is the first study to show, in Escherichia coli, an interaction between a translesion polymerase (PolIV) and a helicase (Rep) normally involved in chromosome replication.
Rep and DnaB helicases remove blocking lesions that would impede normal chromosomal replication. PolIV, the product of the...Continue reading
Rep and DnaB helicases remove blocking lesions that would impede normal chromosomal replication. PolIV, the product of the...Continue reading
This is the first study to show, in Escherichia coli, an interaction between a translesion polymerase (PolIV) and a helicase (Rep) normally involved in chromosome replication.
Rep and DnaB helicases remove blocking lesions that would impede normal chromosomal replication. PolIV, the product of the dinB gene, is a translesion polymerase that contributes substantially to adaptive, but not spontaneous, mutability. It may also play a role in restarting blocked or collapsed replication forks. The authors show that the in vitro interaction of Rep and PolIV stimulates the activity of both and that Rep stimulates PolIV-dependent adaptive mutagenesis.
The authors speculate that since both Rep and PolIV have been implicated in the restart of collapsed replication forks in the PriC-dependent pathway, their role may be to recognize and extend recombinational intermediates during double-strand break repair.
Rep and DnaB helicases remove blocking lesions that would impede normal chromosomal replication. PolIV, the product of the dinB gene, is a translesion polymerase that contributes substantially to adaptive, but not spontaneous, mutability. It may also play a role in restarting blocked or collapsed replication forks. The authors show that the in vitro interaction of Rep and PolIV stimulates the activity of both and that Rep stimulates PolIV-dependent adaptive mutagenesis.
The authors speculate that since both Rep and PolIV have been implicated in the restart of collapsed replication forks in the PriC-dependent pathway, their role may be to recognize and extend recombinational intermediates during double-strand break repair.
Disclosures
None declared
Add Comment
Marinus M: F1000Prime Recommendation of [Sladewski TE et al., Mol Microbiol 2011, 80(2):524-41]. In F1000Prime, 20 May 2011; DOI: 10.3410/f.10652959.11531057. F1000Prime.com/10652959#eval11531057
F1000Prime Recommendations, Dissents and Comments for [Sladewski TE et al., Mol Microbiol 2011, 80(2):524-41]. In F1000Prime, 20 May 2013; F1000Prime.com/10652959
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Escherichia coli DNA polymerase IV, encoded by the dinB gene, is a member of the Y family of specialized DNA polymerases. Pol IV is capable of synthesizing past DNA lesions and may help to restart stalled replication forks. However, Pol IV is error-prone, contributing to both DNA damage-induced and stress-induced (adaptive) mutations. Here we demonstrate that Pol IV interacts in vitro with Rep DNA helicase and that this interaction enhances Rep's helicase activity. In addition, Pol IV polymerase activity is stimulated by interacting with Rep, and Pol IV β clamp-binding motif appears to be required for this stimulation. However, neither Rep's helicase activity nor its ability to bind DNA is required for it to stimulate Pol IV's polymerase activity. The interaction between Rep and Pol IV is biologically significant in vivo as Rep enhances Pol IV's mutagenic activity in stationary-phase cells. These data indicate a new role for Rep in contributing to Pol IV-dependent adaptive mutation. This functional interaction also provides new insight into how the cell might control or target Pol IV's mutagenic activity.
© 2011 Blackwell Publishing Ltd.
DOI: 10.1111/j.1365-2958.2011.07590.x
PMID: 21320186
