RegG, a CcpA Homolog, Participates in Regulation of Amylase-Binding Protein A Gene (abpA) Expression in Streptococcus gordonii
AUTOR(ES)
Rogers, Jeffrey D.
FONTE
American Society for Microbiology
RESUMO
The amylase-binding protein A (AbpA) of Streptococcus gordonii was found to be undetectable in supernatants of mid-log-phase cultures containing >1% glucose but abundant in supernatants of cultures made with brain heart infusion (BHI), which contains 0.2% glucose. A 10-fold decrease in the level of abpA mRNA in S. gordonii cells cultured in BHI was noted after the addition of glucose to 1%. Analysis of the abpA sequence revealed a potential catabolite responsive element CRE 153 bp downstream of the putative translational start site. A catabolite control protein A gene (ccpA) homolog from S. gordonii, designated regG, was cloned. A regG mutant strain demonstrated moderately less repression of abpA transcription in the presence of 1% glucose. Diauxic growth with glucose and lactose was not affected in the RegG mutant compared to the wild-type parental strain. These results suggest that while RegG plays a role in abpA expression, other mechanisms of catabolite repression are present.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=99651Documentos Relacionados
- Prevalence of the Amylase-Binding Protein A Gene (abpA) in Oral Streptococci
- Characterization of an amylase-binding component of Streptococcus gordonii G9B.
- Role of Streptococcus gordonii Amylase-Binding Protein A in Adhesion to Hydroxyapatite, Starch Metabolism, and Biofilm Formation
- Identification of a Homolog of CcpA Catabolite Repressor Protein in Streptococcus mutans
- Control of Expression of the Arginine Deiminase Operon of Streptococcus gordonii by CcpA and Flp