<b>Antitermination of transcription of catabolic operons</b>

Rutberg, Blanka

doi:10.1046/j.1365-2958.1997.d01-1867.x

Cited by 102 publications

(96 citation statements)

References 55 publications

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“…The three fragments hybridized to transcripts of the same size, indicating that the two proteins could be cotranscribed as in other systems (Rutberg, 1997), as illustrated in Fig. 4.…”

Section: Pediocin-resistant L Monocytogenes 412 Mutants Had Increasementioning

confidence: 74%

“…The permeases are in most cases co-transcribed with the downstream phospho-β-glucosidase and the expression is regulated by catabolite repression mediated by the general PTS proteins, and specific induction by the β-glucoside substrates which prevents negative regulation by IIAB (Rutberg, 1997 ;Stu$ lke et al, 1998).…”

Section: Amino Acid Homology Of the Overexpressed Fragmentsmentioning

confidence: 99%

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Restriction fragment differential display of pediocin-resistant Listeria monocytogenes 412 mutants shows consistent overexpression of a putative β-glucoside-specific PTS system The EMBL accession numbers for the sequences reported in this paper are AJ251202, AJ251203 and AJ251204.

Gravesen¹,

Warthoe²,

Knøchel³

et al. 2000

Microbiology

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Pediocin PA-1, which is a bacteriocin produced by lactic acid bacteria, has potential as a biopreservative of food. However, such use may lead to the development of resistance in the target organism. Gene expression in two independent pediocin-resistant mutants of Listeria monocytogenes 412 was compared to the original isolate by restriction fragment differential display PCR (RFDD-PCR). This method amplifies cDNA restriction fragments under stringent PCR conditions, enabled by the use of specific primers complementary to ligated adaptor sequences. RFDD-PCR was very well suited for analysis of listerial gene expression, giving reproducible PCR product profiles. Three gene fragments having increased expression in both resistant mutants were identified. All three had homology to components of β-glucoside-specific phosphoenolpyruvate-dependent phosphotransferase systems (PTS), one fragment having homology to enzyme II permeases, and the two others to phospho-β-glucosidases. Overexpression of the putative PTS system was consistently observed in 10 additional pediocin-resistant mutants, isolated at different pH, salt content and temperature. The results suggest that RFDD-PCR is a strong approach for the analysis of prokaryotic gene expression and that the putative β-glucoside-specific PTS system is involved in mediating pediocin resistance.

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“…The three fragments hybridized to transcripts of the same size, indicating that the two proteins could be cotranscribed as in other systems (Rutberg, 1997), as illustrated in Fig. 4.…”

Section: Pediocin-resistant L Monocytogenes 412 Mutants Had Increasementioning

confidence: 74%

Section: Amino Acid Homology Of the Overexpressed Fragmentsmentioning

confidence: 99%

Restriction fragment differential display of pediocin-resistant Listeria monocytogenes 412 mutants shows consistent overexpression of a putative β-glucoside-specific PTS system The EMBL accession numbers for the sequences reported in this paper are AJ251202, AJ251203 and AJ251204.

Gravesen¹,

Warthoe²,

Knøchel³

et al. 2000

Microbiology

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“…Induction of the two sucrose operons and the ␤-glucoside operon is regulated by transcriptional antitermination. The specific antiterminator proteins (RAT) bind to their respective RNA targets to prevent transcriptional termination at factor-independent terminators (Rutberg, 1997). In the absence of the inducer, the respective EII are thought to transfer their phosphate group to the antiterminator proteins, thereby inactivating them.…”

Section: Introductionmentioning

confidence: 99%

Induction of the Bacillus subtilis ptsGHI operon by glucose is controlled by a novel antiterminator, GlcT

Stülke

Martin‐Verstraete

Zagorec³

et al. 1997

Molecular Microbiology

165

187

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SummaryGlucose is the preferred carbon and energy source of Bacillus subtilis. It is transported into the cell by the glucose-specific phosphoenolpyruvate:sugar phosphotransferase system (PTS) encoded by the ptsGHI locus. We show here that these three genes (ptsG, ptsH, and ptsI ) form an operon, the expression of which is inducible by glucose. In addition, ptsH and ptsI form a constitutive ptsHI operon. The promoter of the ptsGHI operon was mapped and expression from this promoter was found to be constitutive. Deletion mapping of the promoter region revealed the presence of a transcriptional terminator as a regulatory element between the promoter and coding region of the ptsG gene. Mutations within the ptsG gene were characterized and their consequences on the expression of ptsG studied. The results suggest that expression of the ptsGHI operon is subject to negative autoregulation by the glucose permease, which is the ptsG gene product. A regulatory gene located upstream of the ptsGHI operon, termed glcT, was also identified. The GlcT protein is a novel member of the BglG family of transcriptional antiterminators and is essential for the expression of the ptsGHI operon. A deletion of the terminator alleviates the need for GlcT. The activity of GlcT is negatively regulated by the glucose permease.

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“…Antiterminator proteins are believed to be involved in the transcriptional regulation of b-glucoside-specific genes from Escherichia coli (Hall & Xu, 1992), Erwinia chrysanthemi (el Hassouni et al, 1990), Lactococcus lactis (Bardowski et al, 1994), Lactobacillus plantarum (Marasco et al, 2000), B. subtilis (Le Coq et al, 1995;Tobisch et al, 1997) and C. longisporum (Brown & Thomson, 1998). It is believed that these antiterminator proteins would bind to a ribonucleic antiterminator (RAT) site present in a specific mRNA secondary structure and would prevent the formation of a hairpin terminator structure that terminates transcription (Rutberg, 1997). The binding of the antiterminator protein to the mRNA would allow transcription through the disrupted terminator structure into the b-glucoside-specific genes that are not normally transcribed.…”

Section: Introductionmentioning

confidence: 99%

“…The binding of the antiterminator protein to the mRNA would allow transcription through the disrupted terminator structure into the b-glucoside-specific genes that are not normally transcribed. Thus, the antitermination mechanism of transcriptional regulation allows for the expression of b-glucoside-specific loci in the absence of a metabolically preferred carbon source (Rutberg, 1997).…”

Section: Introductionmentioning

confidence: 99%

The LicT protein acts as both a positive and a negative regulator of loci within the bgl regulon of Streptococcus mutans

Cote

Honeyman

2003

Microbiology

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An open reading frame (ORF) that would encode a putative antiterminator protein (LicT) of the BglG family was identified in the genomic DNA sequence of Streptococcus mutans. A DNA sequence that would encode a potential ribonucleic antiterminator (RAT) site in the mRNA at which the putative antitermination protein LicT would bind was located immediately downstream from this ORF. These putative antitermination components are upstream of a glucose-independent b-glucoside-utilization system that is responsible for aesculin utilization by S. mutans NG8 in the presence of glucose. It was hypothesized that these putative regulatory components were an important mechanism that was involved with the controlled expression of the S. mutans bglP locus. A strain of S. mutans containing a licT : : V-Kan2 insertional mutation was created. This strain could not hydrolyse aesculin in the presence of glucose. The transcriptional activity associated with other genes from the bgl regulon was determined in the licT : : V-Kan2 genetic background using lacZ transcriptional fusions and b-galactosidase assays to determine the effect of LicT on these loci. The LicT protein had no significant effect on the expression of the bglC promoter, a regulator of the bglA locus. However, it is essential for the optimal expression of bglP. These data correlate with the phenotype observed on aesculin plates for the S. mutans wild-type strain NG8 and the licT : : V-Kan2 strain. Thus, the glucose-independent b-glucoside-specific phosphotransferase system (PTS) regulon in S. mutans relies on LicT for BglP expression and, in turn, aesculin transport in the presence of glucose. Interestingly, LicT also seems to negatively regulate the expression of the bglA promoter region. In addition, the presence of the S. mutans licT gene has been shown to be able to activate a cryptic b-glucoside-specific operon found in Escherichia coli.

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Antitermination of transcription of catabolic operons

Cited by 102 publications

References 55 publications

Restriction fragment differential display of pediocin-resistant Listeria monocytogenes 412 mutants shows consistent overexpression of a putative β-glucoside-specific PTS system The EMBL accession numbers for the sequences reported in this paper are AJ251202, AJ251203 and AJ251204.

Restriction fragment differential display of pediocin-resistant Listeria monocytogenes 412 mutants shows consistent overexpression of a putative β-glucoside-specific PTS system The EMBL accession numbers for the sequences reported in this paper are AJ251202, AJ251203 and AJ251204.

Induction of the Bacillus subtilis ptsGHI operon by glucose is controlled by a novel antiterminator, GlcT

The LicT protein acts as both a positive and a negative regulator of loci within the bgl regulon of Streptococcus mutans

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