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A physical and functional analysis of the newly-identified bglGPT operon of Lactobacillus plantarum
- Source :
- FEMS microbiology letters. 186(2)
- Publication Year :
- 2000
-
Abstract
- A newly-identified bglGPT operon of Lactobacillus plantarum was isolated and expressed in Escherichia coli. The sequence analysis of the cloned DNA fragment showed three open reading frames encoding (i) a 237-amino acid protein (BglG), (ii) a 577-amino acid protein (BglP) and (iii) a 486-amino acid protein (BglT). BglG, BglP and BglT were shown to be homologous to the BglG family of transcriptional antiterminators, to permeases of the phosphoenolpyruvate-dependent phosphotransferase system and to β-glucosidases, respectively. Complementation of E. coli mutant strains showed that BglP and BglT are a permease and a β-glucosidase active on the β-glucosides, 5-bromo-4-chloro-3-indolyl-β-D-glucopyranoside and p-nitrophenyl-β-D-glucoside, respectively. BglG was also shown to promote expression of a bglG-lacZ gene fusion in an E. coli bglG- background. A ribonucleic antiterminator sequence, the antiterminator-responsive cis-element and a 'catabolite responsive element', were found downstream of the transcriptional start point. Transcription of the operon was repressed 10-fold in L. plantarum cells grown on glucose as compared to ribose. Copyright (C) 2000 Federation of European Microbiological Societies.
- Subjects :
- Operon
Sequence analysis
Molecular Sequence Data
Catabolite repression
bglGPT operon
Biology
medicine.disease_cause
Microbiology
Open Reading Frames
Bacterial Proteins
Genetics
medicine
Escherichia coli
Cloning, Molecular
Phosphoenolpyruvate Sugar Phosphotransferase System
Molecular Biology
Lactobacillu
Base Sequence
Permease
beta-Glucosidase
Membrane Transport Proteins
RNA-Binding Proteins
PEP group translocation
Recombinant Proteins
β-Glucosidase
Complementation
Open reading frame
Lactobacillus
RNA, Bacterial
Biochemistry
Carbon-catabolite repression
Plasmids
Subjects
Details
- ISSN :
- 03781097
- Volume :
- 186
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- FEMS microbiology letters
- Accession number :
- edsair.doi.dedup.....d34d9979ac72f6eea818aff384b9068a