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. 2001 Jun;183(11):3521-5.
doi: 10.1128/JB.183.11.3521-3525.2001.

"V体育2025版" RegG, a CcpA homolog, participates in regulation of amylase-binding protein A gene (abpA) expression in Streptococcus gordonii

J D Rogers  1 , F A Scannapieco
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RegG, a CcpA homolog, participates in regulation of amylase-binding protein A gene (abpA) expression in Streptococcus gordonii

"VSports注册入口" J D Rogers et al. J Bacteriol. 2001 Jun.

Abstract (VSports手机版)

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 VSports手机版. 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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Figures

FIG. 1
FIG. 1
(A) Influence of carbohydrate source on AbpA expression. A solid-phase amylase ligand-binding assay was carried out with culture supernatants (100 μg per lane) of S. gordonii Challis grown in defined medium with 1% concentrations of the following sugars: glucose (lane 2), lactose (lane 4), maltose (lane 5), and maltooligosaccharides (lane 6). Lane 1 contains molecular mass standards, and lane 3 is a positive control (BHI with no added sugar). The blot was first probed with purified amylase followed by rabbit antiamylase. Bound antibodies were visualized using goat-anti rabbit immunoglobulin G conjugated to an alkaline phosphatase reporter. (B) Northern blot of cells grown in BHI supplemented with 1% glucose (lane 1) or BHI with no added sugar (positive control) (lane 2). The Northern blot was probed with biotinylated abpA.
FIG. 2
FIG. 2
Time course study of abpA mRNA transcript levels. (A) Total RNA (5 μg) was isolated from S. gordonii at mid-logarithmic growth (lane 1) and at 2 min (lane 2), 5 min (lane 3), 10 min (lane 4), and 15 min (lane 5) after the addition of 1% glucose to the culture. (B) Total RNA from parallel cultures grown without additional glucose is included for comparison. Biotinylated abpA was used as the probe.
FIG. 3
FIG. 3
Sequence analysis of the regG locus. The nucleotide and deduced amino acid sequences are given for regG. The ribosome binding site (RBS) and the −10 and −35 promoter elements for regG are indicated, as is the NdeI restriction site used for insertion of the ermAM gene and inactivation of regG. The nucleotides corresponding to the pepQ partial open reading frame are also indicated, with the putative translational start site underlined.
FIG. 4
FIG. 4
Transcriptional regulation of abpA by RegG. Total RNA was extracted from S. gordonii Challis (lanes 1 and 2) and Challis-CE1 (lanes 3 and 4) during exponential growth in BHI (lanes 1 and 3) or in BHI supplemented with 1% glucose (lanes 2 and 4). As a reference, sequencing reactions using the same primer (PE1) were performed (left).
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V体育安卓版 - References

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