RegG, a CcpA homolog, participates in regulation of amylase-binding protein A gene (abpA) expression in Streptococcus gordonii

Journal of Bacteriology
J D Rogers, F A Scannapieco

Abstract

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.

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Citations

Mar 8, 2012·Molecular Oral Microbiology·L ZhengJ Kreth
Jul 5, 2012·Molecular Oral Microbiology·A E NikitkovaF A Scannapieco
May 17, 2011·Applied and Environmental Microbiology·Lanyan ZhengJens Kreth
Jan 18, 2011·Applied and Environmental Microbiology·Huichun TongRobert A Burne
Sep 2, 2009·Microbiology and Molecular Biology Reviews : MMBR·Angela H NobbsHoward F Jenkinson
Dec 13, 2006·Microbiology and Molecular Biology Reviews : MMBR·Josef DeutscherPieter W Postma
Sep 21, 2007·Molecular Microbiology·Ramkumar Iyer, Andrew Camilli
May 31, 2015·Applied and Environmental Microbiology·Elaine M HaaseFrank A Scannapieco

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