UMMS Affiliation

Department of Microbiology and Physiological Systems

Date

3-31-2011

Document Type

Article

Subjects

Escherichia coli; Escherichia coli Proteins; *Mutation; Phenotype; Rec A Recombinases; *Recombination, Genetic; Transcription Factors

Disciplines

Biochemistry, Biophysics, and Structural Biology | Life Sciences | Medicine and Health Sciences

Abstract

BACKGROUND: The elongation factor GreA binds to RNA polymerase and modulates transcriptional pausing. Some recent research suggests that the primary role of GreA may not be to regulate gene expression, but rather, to promote the progression of replication forks which collide with RNA polymerase, and which might otherwise collapse. Replication fork collapse is known to generate dsDNA breaks, which can be recombinogenic. It follows that GreA malfunction could have consequences affecting homologous recombination.

RESULTS: Escherichia coli mutants bearing substitutions of the active site acidic residues of the transcription elongation factor GreA, D41N and E44K, were isolated as suppressors of growth inhibition by a toxic variant of the bacteriophage lambda Red-beta recombination protein. These mutants, as well as a D41A greA mutant and a greA deletion, were tested for proficiency in recombination events. The mutations were found to increase the efficiency of RecA-RecBCD-mediated and RecA-Red-mediated recombination, which are replication-independent, and to decrease the efficiency of replication-dependent Red-mediated recombination.

CONCLUSION: These observations provide new evidence for a role of GreA in resolving conflicts between replication and transcription.

Rights and Permissions

Citation: BMC Mol Biol. 2011 Mar 31;12:12. Link to article on publisher's site

DOI of Published Version

10.1186/1471-2199-12-12

Comments

© 2011 Poteete; licensee BioMed Central Ltd.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Related Resources

Link to Article in PubMed

Journal Title

BMC molecular biology

PubMed ID

21453489

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