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Journal of Bacteriology, June 2001, p. 3521-3525, Vol. 183, No. 11
Department of Oral Biology, School of Dental
Medicine, University at Buffalo, The State University of New York,
Buffalo, New York 14214
Received 20 November 2000/Accepted 12 January 2001
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.
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.11.3521-3525.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
RegG, a CcpA Homolog, Participates in Regulation of
Amylase-Binding Protein A Gene (abpA) Expression in
Streptococcus gordonii
and
*
Corresponding author. Mailing address: 109 Foster Hall,
School of Dental Medicine, University at Buffalo, The State University of New York, Buffalo, NY 14214. Phone: (716) 829-3373. Fax: (716) 829-3942. E-mail: fas1{at}acsu.buffalo.edu.
Present address: Department of Periodontics, School of Dentistry,
Virginia Commonwealth University, Richmond, VA 23298-0566.
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