DNA Helicase Activity of PcrA Is Not Required for the Displacement of RecA Protein from DNA or Inhibition of RecA-Mediated Strand Exchange

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Published inJournal of Bacteriology Vol. 189; no. 12; pp. 4502 - 4509
Main Authors Anand, Syam P, Zheng, Haocheng, Bianco, Piero R, Leuba, Sanford H, Khan, Saleem A
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for Microbiology 01.06.2007
Subjects
Bacterial Proteins - genetics
Bacterial Proteins - physiology
Bacteriology
Biological and medical sciences
Deoxyribonucleic acid
DNA
DNA Helicases - genetics
DNA Helicases - physiology
DNA, Bacterial - metabolism
DNA, Single-Stranded - metabolism
Enzymes and Proteins
Fluorescence Resonance Energy Transfer
Fundamental and applied biological sciences. Psychology
Gram-positive bacteria
Gram-Positive Bacteria - enzymology
Gram-Positive Bacteria - genetics
Gram-Positive Bacteria - physiology
Microbiology
Miscellaneous
Mutation
Proteins
Rec A Recombinases - antagonists & inhibitors
Rec A Recombinases - metabolism
Recombination, Genetic - physiology
Microbiology
RecA protein
Bacteriology
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Abstract Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0021-9193 Online ISSN: 1098-5530 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JB .asm.org, visit: JB       
AbstractList PcrA is a conserved DNA helicase present in all gram-positive bacteria. Bacteria lacking PcrA show high levels of recombination. Lethality induced by PcrA depletion can be overcome by suppressor mutations in the recombination genes recFOR. RecFOR proteins load RecA onto single-stranded DNA during recombination. Here we test whether an essential function of PcrA is to interfere with RecA-mediated DNA recombination in vitro. We demonstrate that PcrA can inhibit the RecA-mediated DNA strand exchange reaction in vitro. Furthermore, PcrA displaced RecA from RecA nucleoprotein filaments. Interestingly, helicase mutants of PcrA also displaced RecA from DNA and inhibited RecA-mediated DNA strand exchange. Employing a novel single-pair fluorescence resonance energy transfer-based assay, we demonstrate a lengthening of double-stranded DNA upon polymerization of RecA and show that PcrA and its helicase mutants can reverse this process. Our results show that the displacement of RecA from DNA by PcrA is not dependent on its translocase activity. Further, our results show that the helicase activity of PcrA, although not essential, might play a facilitatory role in the RecA displacement reaction.
ABSTRACT PcrA is a conserved DNA helicase present in all gram-positive bacteria. Bacteria lacking PcrA show high levels of recombination. Lethality induced by PcrA depletion can be overcome by suppressor mutations in the recombination genes recFOR . RecFOR proteins load RecA onto single-stranded DNA during recombination. Here we test whether an essential function of PcrA is to interfere with RecA-mediated DNA recombination in vitro. We demonstrate that PcrA can inhibit the RecA-mediated DNA strand exchange reaction in vitro. Furthermore, PcrA displaced RecA from RecA nucleoprotein filaments. Interestingly, helicase mutants of PcrA also displaced RecA from DNA and inhibited RecA-mediated DNA strand exchange. Employing a novel single-pair fluorescence resonance energy transfer-based assay, we demonstrate a lengthening of double-stranded DNA upon polymerization of RecA and show that PcrA and its helicase mutants can reverse this process. Our results show that the displacement of RecA from DNA by PcrA is not dependent on its translocase activity. Further, our results show that the helicase activity of PcrA, although not essential, might play a facilitatory role in the RecA displacement reaction.
PcrA is a conserved DNA helicase present in all gram-positive bacteria. Bacteria lacking PcrA show high levels of recombination. Lethality induced by PcrA depletion can be overcome by suppressor mutations in the recombination genes recFOR. RecFOR proteins load RecA onto single-stranded DNA during recombination. Here we test whether an essential function of PcrA is to interfere with RecA- mediated DNA recombination in vitro. We demonstrate that PcrA can inhibit the RecA-mediated DNA strand exchange reaction in vitro. Furthermore, PcrA displaced RecA from RecA nucleoprotein filaments. Interestingly, helicase mutants of PcrA also displaced RecA from DNA and inhibited RecA- mediated DNA strand exchange. Employing a novel single-pair fluorescence resonance energy transfer- based assay, we demonstrate a lengthening of double-stranded DNA upon polymerization of RecA and show that PcrA and its helicase mutants can reverse this process. Our results show that the displacement of RecA from DNA by PcrA is not dependent on its translocase activity. Further, our results show that the helicase activity of PcrA, although not essential, might play a facilitatory role in the RecA displacement reaction. [PUBLICATION ABSTRACT]
PcrA is a conserved DNA helicase present in all gram-positive bacteria. Bacteria lacking PcrA show high levels of recombination. Lethality induced by PcrA depletion can be overcome by suppressor mutations in the recombination genes recFOR . RecFOR proteins load RecA onto single-stranded DNA during recombination. Here we test whether an essential function of PcrA is to interfere with RecA-mediated DNA recombination in vitro. We demonstrate that PcrA can inhibit the RecA-mediated DNA strand exchange reaction in vitro. Furthermore, PcrA displaced RecA from RecA nucleoprotein filaments. Interestingly, helicase mutants of PcrA also displaced RecA from DNA and inhibited RecA-mediated DNA strand exchange. Employing a novel single-pair fluorescence resonance energy transfer-based assay, we demonstrate a lengthening of double-stranded DNA upon polymerization of RecA and show that PcrA and its helicase mutants can reverse this process. Our results show that the displacement of RecA from DNA by PcrA is not dependent on its translocase activity. Further, our results show that the helicase activity of PcrA, although not essential, might play a facilitatory role in the RecA displacement reaction.
Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0021-9193 Online ISSN: 1098-5530 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JB .asm.org, visit: JB       
Author Piero R. Bianco
Syam P. Anand
Saleem A. Khan
Haocheng Zheng
Sanford H. Leuba
AuthorAffiliation Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261, 1 Department of Cell Biology and Physiology, University of Pittsburgh School of Medicine, and University of Pittsburgh Cancer Institute, Pittsburgh, Pennsylvania 15261, 2 Department of Microbiology and Immunology, Center for Single Molecule Biophysics, University at Buffalo, Buffalo, New York 14214 3
AuthorAffiliation_xml – name: Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261, 1 Department of Cell Biology and Physiology, University of Pittsburgh School of Medicine, and University of Pittsburgh Cancer Institute, Pittsburgh, Pennsylvania 15261, 2 Department of Microbiology and Immunology, Center for Single Molecule Biophysics, University at Buffalo, Buffalo, New York 14214 3
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Corresponding author. Mailing address: East 1240 Biomedical Science Tower, 200 Lothrop Street, Pittsburgh, PA 15261. Phone: (412) 648-9025. Fax: (412) 624-1401. E-mail: khan@pitt.edu
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PcrA is a conserved DNA helicase present in all gram-positive bacteria. Bacteria lacking PcrA show high levels of recombination. Lethality induced by PcrA...
ABSTRACT PcrA is a conserved DNA helicase present in all gram-positive bacteria. Bacteria lacking PcrA show high levels of recombination. Lethality induced by...
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StartPage 4502
SubjectTerms Bacterial Proteins - genetics
Bacterial Proteins - physiology
Bacteriology
Biological and medical sciences
Deoxyribonucleic acid
DNA
DNA Helicases - genetics
DNA Helicases - physiology
DNA, Bacterial - metabolism
DNA, Single-Stranded - metabolism
Enzymes and Proteins
Fluorescence Resonance Energy Transfer
Fundamental and applied biological sciences. Psychology
Gram-positive bacteria
Gram-Positive Bacteria - enzymology
Gram-Positive Bacteria - genetics
Gram-Positive Bacteria - physiology
Microbiology
Miscellaneous
Mutation
Proteins
Rec A Recombinases - antagonists & inhibitors
Rec A Recombinases - metabolism
Recombination, Genetic - physiology
Title DNA Helicase Activity of PcrA Is Not Required for the Displacement of RecA Protein from DNA or Inhibition of RecA-Mediated Strand Exchange
URI http://jb.asm.org/content/189/12/4502.abstract
https://www.ncbi.nlm.nih.gov/pubmed/17449621
https://www.proquest.com/docview/227078665
https://search.proquest.com/docview/20349831
https://search.proquest.com/docview/70574540
https://pubmed.ncbi.nlm.nih.gov/PMC1913354
Volume 189
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