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

Academic Article


  • A spontaneous mutant of Streptococcus pneumoniae strain D39 exhibiting elevated β-galactosidase activity was identified. We determined that the β-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 β-galactosidase (BgaAC) mutant, but not in the parent. β-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 catabolite-responsive element (cre) and affected the binding of CcpA (catabolite control protein A), a key regulator of many carbon metabolism genes. The pts operon and bgaA were cotranscribed, and their transcription was regulated by CcpA. Deletion of ccpA altered β-galactosidase activity, leading to a sevenfold increase in the parent but a fivefold decrease in the BgaAC mutant. The resulting β-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 the glucose concentration. Expression of β-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. Copyright © 2007, American Society for Microbiology. All Rights Reserved.
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    Author List

  • Kaufman GE; Yother J
  • Start Page

  • 5183
  • End Page

  • 5192
  • Volume

  • 189
  • Issue

  • 14