Document Detail

CodY is a nutritional repressor of flagellar gene expression in Bacillus subtilis.
MedLine Citation:
PMID:  12730172     Owner:  NLM     Status:  MEDLINE    
Expression of the sigma(D)-dependent flagellin gene, hag, is repressed by the CodY protein in nutrient-rich environments. Analysis of a codY mutant bearing a hag-lacZ reporter suggests that the availability of amino acids in the environment is the specific signal that triggers this repression. Further, hag-lacZ expression appears to be sensitive to intracellular GTP levels, as demonstrated by increased expression upon addition of decoyinine. This result is consistent with the postulate that the availability of amino acids in the environment effects intracellular GTP levels through the stringent response. However, the levels of hag-lacZ measured upon the addition of subsets of amino acids suggest an additional mechanism(s). CodY is a DNA binding protein that could repress flagellin expression directly by binding to the hag promoter region, or indirectly by binding to the fla/che promoter region that governs expression of the sigma(D) transcriptional activator required for hag gene expression. Using an electrophoretic mobility shift assay, we have demonstrated that purified CodY protein binds specifically to both the hag and fla/che promoter fragments. Additionally, CodY acts as a nutritional repressor of transcription from the fla/che promoter region that contains two functional promoters. CodY binds to both the sigma(D)- and sigma(A)-dependent promoters in this region, as demonstrated by DNase I footprint analyses. Footprint analyses of the hag gene demonstrated that CodY binds downstream of its sigma(D)-dependent promoter. Taken together, these results identify new members of the CodY regulon that encode motility functions in Bacillus subtilis and are controlled by the sigma(D) alternate sigma factor.
F Bergara; C Ibarra; J Iwamasa; J C Patarroyo; R Aguilera; L M Márquez-Magaña
Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of bacteriology     Volume:  185     ISSN:  0021-9193     ISO Abbreviation:  J. Bacteriol.     Publication Date:  2003 May 
Date Detail:
Created Date:  2003-05-05     Completed Date:  2003-06-16     Revised Date:  2013-04-18    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3118-26     Citation Subset:  IM    
Department of Biology, San Francisco State University, San Francisco, California 94132, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Amino Acids, Branched-Chain / metabolism,  pharmacology
Bacillus subtilis / drug effects,  genetics*,  metabolism
Bacterial Proteins / genetics,  metabolism,  physiology*
Base Sequence
Binding Sites
Culture Media
DNA Footprinting
DNA-Binding Proteins / physiology*
Flagella / genetics*
Flagellin / genetics*,  metabolism
Gene Expression Regulation, Bacterial*
Guanosine Triphosphate / metabolism
Molecular Sequence Data
Peptide Synthases / genetics,  metabolism
Promoter Regions, Genetic
Recombinant Proteins / genetics,  metabolism
Repressor Proteins / physiology*
Sigma Factor / genetics
Transcription Factors / genetics,  metabolism
beta-Galactosidase / genetics,  metabolism
Grant Support
Reg. No./Substance:
0/Amino Acids, Branched-Chain; 0/Bacterial Proteins; 0/Culture Media; 0/DNA-Binding Proteins; 0/Recombinant Proteins; 0/Repressor Proteins; 0/Sigma Factor; 0/Transcription Factors; 12777-81-0/Flagellin; 155490-96-3/comK protein, Bacillus subtilis; 86-01-1/Guanosine Triphosphate; EC; EC 6.3.2.-/Peptide Synthases; EC 6.3.2.-/surfactin synthetase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Swarm-cell differentiation in Salmonella enterica serovar typhimurium results in elevated resistance...
Next Document:  Characterization of NorR protein, a multifunctional regulator of norA expression in Staphylococcus a...