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Department of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294
* To whom correspondence should be addressed. Email:
jyother{at}uab.edu.
A spontaneous mutant of Streptococcus pneumoniae strain D39 exhibiting elevated
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
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Abstract
-galactosidase activity was identified. We determined that
-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
-galactosidase (BgaAC) mutant but not in the parent.
-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
-galactosidase activity, leading to a 7-fold increase in the parent but a 5-fold decrease in the BgaAC mutant. The resulting
-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
-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.
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