Document Detail


The role of proton motive force in expression of the Staphylococcus aureus cid and lrg operons.
MedLine Citation:
PMID:  16468984     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The Staphylococcus aureus cidABC and lrgAB operons have been shown to play a key role in the regulation of murein hydrolase activity and cell death in a manner thought to be analogous to bacteriophage-encoded holins and anti-holins respectively. Because of these functions, it has been proposed that the regulation of these operons is tightly controlled and responsive to key metabolic signals. The current study revealed the presence of two overlapping regulatory pathways controlling cidABC and lrgAB expression, one dependent on acetic acid and the other dependent on proton motive force (PMF). The latter pathway was analysed using agents that affect various aspects of the PMF. Gramicidin and carbonyl cyanide m-chlorophenylhydrazone (CCCP), antimicrobial agents that dissipate the DeltapH and membrane potential (DeltaPsi), both enhanced lrgAB expression. Restoration of the PMF by incubation of the bacteria in the presence of glucose restored lrgAB expression back to the uninduced state. In addition, valinomycin, which specifically collapses the DeltaPsi, also induced lrgAB expression. In contrast, nigericin, which dissipates the DeltapH component of the PMF, was found to have a minimal effect on DeltaPsi and lrgAB transcription. Finally, the DeltaPsi-inducible expression of lrgAB was shown to be dependent on the previously characterized LytSR two-component regulatory system that is involved in the regulation of autolysis. The results of this study support a model in which the LytSR regulatory system responds to a collapse in DeltaPsi by inducing the transcription of the lrgAB operon.
Authors:
Toni G Patton; Soo-Jin Yang; Kenneth W Bayles
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Molecular microbiology     Volume:  59     ISSN:  0950-382X     ISO Abbreviation:  Mol. Microbiol.     Publication Date:  2006 Mar 
Date Detail:
Created Date:  2006-02-10     Completed Date:  2006-05-02     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  8712028     Medline TA:  Mol Microbiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  1395-404     Citation Subset:  IM    
Affiliation:
Department of Microbiology, Molecular Biology and Biochemistry, University of Idaho, Moscow, 83844-3052, USA.
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MeSH Terms
Descriptor/Qualifier:
Acids / pharmacology
Anti-Infective Agents / pharmacology
Bacterial Proteins / drug effects,  genetics,  metabolism
Carbonyl Cyanide m-Chlorophenyl Hydrazone / pharmacology
Gene Expression Regulation, Bacterial* / drug effects
Gramicidin / pharmacology
Membrane Potentials / drug effects
Nigericin / pharmacology
Operon*
Proton-Motive Force / genetics*
Staphylococcus aureus / drug effects,  genetics*
Transcription Factors / drug effects
Transcription, Genetic
Valinomycin / pharmacology
Grant Support
ID/Acronym/Agency:
P20RR15587/RR/NCRR NIH HHS; R01AI038901/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Acids; 0/Anti-Infective Agents; 0/Bacterial Proteins; 0/LytR protein, Staphylococcus aureus; 0/LytS protein, Staphylococcus aureus; 0/Transcription Factors; 1405-97-6/Gramicidin; 2001-95-8/Valinomycin; 28380-24-7/Nigericin; 555-60-2/Carbonyl Cyanide m-Chlorophenyl Hydrazone

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


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