JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] --
JB Accepts, published online ahead of print on 11 May 2007
This Article
Right arrow Full Text (PDF)
Right arrow Other Versions of this Article:
JB.00449-07v1
189/14/5183    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kaufman, G. E.
Right arrow Articles by Yother, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kaufman, G. E.
Right arrow Articles by Yother, J.

 Previous Article  |  Next Article 

J. Bacteriol. doi:10.1128/JB.00449-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

CcpA-dependent and -independent control of beta-galactosidase expression in Streptococcus pneumoniae occurs via regulation of an upstream PTS-encoding operon

Greer E. Kaufman and Janet Yother*

Department of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294

* To whom correspondence should be addressed. Email: jyother{at}uab.edu.


   Abstract

A spontaneous mutant of Streptococcus pneumoniae strain D39 exhibiting elevated {beta}-galactosidase activity was identified. We determined that {beta}-galactosidase activity was due to BgaA, a surface protein in S. pneumoniae, and that the expression of bgaA was regulated. Transcription analyses demonstrated expression of bgaA in the constitutive {beta}-galactosidase (BgaAC) mutant but not in the parent. {beta}-galactosidase expression was induced in the parent under specific growth conditions, however the levels did not reach those of the BgaAC mutant. We localized the mutation resulting in the BgaAC phenotype to a region upstream of bgaA and in the promoter of a phosphoenolpyruvate-dependent phosphotransferase system (PTS) operon. The mutation was in a cre and affected binding of CcpA (catabolite control protein A), a key regulator of many carbon metabolism genes. The pts operon and bgaA were co-transcribed, and their transcription was regulated by CcpA. Deletion of ccpA altered {beta}-galactosidase activity, leading to a 7-fold increase in the parent but a 5-fold decrease in the BgaAC mutant. The resulting {beta}-galactosidase activities were the same in the two strains, suggesting the presence of a second repressor. The presence of glucose in the growth medium resulted in pts-bgaA repression by both CcpA and the second repressor, with the latter being important in responding to glucose concentration. Expression of {beta}-galactosidase is important for S. pneumoniae adherence during colonization of the nasopharynx, a site normally devoid of glucose. CcpA and environmental glucose concentrations thus appear to play important roles in the regulation of a niche-specific virulence factor.




This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 2007 by the American Society for Microbiology. All rights reserved.