Identification of Conserved Amino Acid Residues of the Salmonella σS Chaperone Crl Involved in Crl-σS Interactions

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Published in:	Journal of Bacteriology Vol. 192; no. 4; pp. 1075 - 1087
Main Authors:	MONTEIL, Véronique, KOLB, Annie, D'ALAYER, Jacques, BEGUIN, Pierre, NOREL, Françoise
Format:	Journal Article
Language:	English
Published:	Washington, DC American Society for Microbiology 15-02-2010 American Society for Microbiology (ASM)
Subjects:	Bacteriology Biological and medical sciences Fundamental and applied biological sciences. Psychology Genetics and Molecular Biology Microbiology Miscellaneous Salmonella Bacteria Identification Chaperone Protein Enterobacteriaceae
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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	Proteins that bind σ factors typically attenuate the function of the σ factor by restricting its access to the RNA polymerase (RNAP) core enzyme. An exception to this general rule is the Crl protein that binds the stationary-phase sigma factor σ S (RpoS) and enhances its affinity for the RNAP core enzyme, thereby increasing expression of σ S -dependent genes. Analyses of sequenced bacterial genomes revealed that crl is less widespread and less conserved at the sequence level than rpoS. Seventeen residues are conserved in all members of the Crl family. Site-directed mutagenesis of the crl gene from Salmonella enterica serovar Typhimurium and complementation of a Δ crl mutant of Salmonella indicated that substitution of the conserved residues Y22, F53, W56, and W82 decreased Crl activity. This conclusion was further confirmed by promoter binding and abortive transcription assays. We also used a bacterial two-hybrid system (BACTH) to show that the four substitutions in Crl abolish Crl-σ S interaction and that residues 1 to 71 in σ S are dispensable for Crl binding. In Escherichia coli , it has been reported that Crl also interacts with the ferric uptake regulator Fur and that Fur represses crl transcription. However, the Salmonella Crl and Fur proteins did not interact in the BACTH system. In addition, a fur mutation did not have any significant effect on the expression level of Crl in Salmonella. These results suggest that the relationship between Crl and Fur is different in Salmonella and E. coli . 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	Annie Kolb Pierre Beguin Françoise Norel Jacques D'Alayer Véronique Monteil
AuthorAffiliation	Unité de Génétique Moléculaire and CNRS URA2172, 1 Plate-Forme d'Analyse et de Microséquençage des Protéines, 2 PF5 Production de Protéines Recombinantes et d'Anticorps, Institut Pasteur, 25-28 rue du Dr Roux, 75724 Paris Cedex 15, France 3
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Author_xml	– sequence: 1 givenname: Véronique surname: MONTEIL fullname: MONTEIL, Véronique organization: Unité de Génétique Moléculaire and CNRS URA2172, Institut Pasteur, 25-28 rue du Dr Roux, 75724 Paris, France – sequence: 2 givenname: Annie surname: KOLB fullname: KOLB, Annie organization: Unité de Génétique Moléculaire and CNRS URA2172, Institut Pasteur, 25-28 rue du Dr Roux, 75724 Paris, France – sequence: 3 givenname: Jacques surname: D'ALAYER fullname: D'ALAYER, Jacques organization: Plate-Forme d'Analyse et de Microséquençage des Protéines, Institut Pasteur, 25-28 rue du Dr Roux, 75724 Paris, France – sequence: 4 givenname: Pierre surname: BEGUIN fullname: BEGUIN, Pierre organization: PF5 Production de Protéines Recombinantes et d'Anticorps, Institut Pasteur, 25-28 rue du Dr Roux, 75724 Paris, France – sequence: 5 givenname: Françoise surname: NOREL fullname: NOREL, Françoise organization: Unité de Génétique Moléculaire and CNRS URA2172, Institut Pasteur, 25-28 rue du Dr Roux, 75724 Paris, France
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Snippet	Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... Proteins that bind σ factors typically attenuate the function of the σ factor by restricting its access to the RNA polymerase (RNAP) core enzyme. An exception...
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SubjectTerms	Bacteriology Biological and medical sciences Fundamental and applied biological sciences. Psychology Genetics and Molecular Biology Microbiology Miscellaneous
Title	Identification of Conserved Amino Acid Residues of the Salmonella σS Chaperone Crl Involved in Crl-σS Interactions
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