Thiol-disulfide oxidoreductases are essential for the production of the lantibiotic sublancin 168

Autor: Albert Bolhuis, Ronald Dorenbos, Torsten Stein, Sierd Bron, Jorrit Kabel, Wim J. Quax, Claude Bruand, Jan Maarten van Dijl
Přispěvatelé: Nanotechnology and Biophysics in Medicine (NANOBIOMED), Biopharmaceuticals, Discovery, Design and Delivery (BDDD), Unité de recherche Génétique Microbienne (UGM), Institut National de la Recherche Agronomique (INRA)
Jazyk: angličtina
Rok vydání: 2002
Předmět:
Cytoplasm
GENE-CLUSTER
Operon
[SDV]Life Sciences [q-bio]
PROTEIN
Peptide
bacillus subtillis
Bacillus subtilis
BATERIE
Biochemistry
Substrate Specificity
antibiotique
chemistry.chemical_compound
Bacteriocins
NUCLEOTIDE-SEQUENCE
Gene cluster
PEPTIDE
Disulfides
lantibiotique
BACILLUS-SUBTILIS ATCC-6633
chemistry.chemical_classification
0303 health sciences
biology
adn
Glycopeptides
Natural competence
Anti-Bacterial Agents
protéine
Plasmids
GRAM-POSITIVE BACTERIA
Molecular Sequence Data
IMMUNITY
pont disulfide
GENETIQUE
03 medical and health sciences
Bacterial Proteins
cytoplasme
thioldisulfite oxydoreductase
LACTOCOCCUS-LACTIS
Molecular Biology
030304 developmental biology
microorganisme
Base Sequence
030306 microbiology
Cell Membrane
Lactococcus lactis
Protein Disulfide Reductase (Glutathione)
oxydoréduction
DNA
Cell Biology
MASS-SPECTROMETRY
Lantibiotics
biology.organism_classification
Protein Structure
Tertiary
NISIN
enzyme
chemistry
Spectrometry
Mass
Matrix-Assisted Laser Desorption-Ionization
ATP-Binding Cassette Transporters
Peptides
Zdroj: The Journal of Biological Chemistry, 277(19), 16682-16688. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2002, 277 (19), pp.16682-16688
Journal of Biological Chemistry 19 (277), 16682-16688. (2002)
ISSN: 1083-351X
0021-9258
DOI: 10.1074/jbc.M201158200
Popis: Thiol-disulfide oxidoreductases are required for disulfide bond formation in proteins that are exported from the cytoplasm. Four enzymes of this type, termed BdbA, BdbB, BdbC, and BdbD, have been identified in the Gram-positive eubacterium Bacillus subtilis. BdbC and BdbD have been shown to be critical for the folding of a protein required for DNA uptake during natural competence. In contrast, no function has been assigned so far to the BdbA and BdbB proteins. The bdbA and bdbB genes are located in one operon that also contains the genes specifying the lantibiotic sublancin 168 and the ATP-binding cassette transporter SunT. Interestingly sublancin 168 contains two disulfide bonds. The present studies demonstrate that SunT and BdbB, but not BdbA, are required for the production of active sublancin 168. In addition, the BdbB paralogue BdbC is at least partly able to replace BdbB in sublancin 168 production. These observations show the unprecedented involvement of thiol-disulfide oxidoreductases in the synthesis of a peptide antibiotic. Notably BdbB cannot complement BdbC in competence development, showing that these two closely related thiol-disulfide oxidoreductases have different, but partly overlapping, substrate specificities.
Databáze: OpenAIRE
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