Thiol-disulfide oxidoreductases are essential for the production of the lantibiotic sublancin 168.
about
Sublancin is not a lantibiotic but an S-linked glycopeptideDisulfide-Bond-Forming Pathways in Gram-Positive BacteriaStaphylococcus aureus DsbA does not have a destabilizing disulfide. A new paradigm for bacterial oxidative foldingStructure analysis of the extracellular domain reveals disulfide bond forming-protein properties of Mycobacterium tuberculosis Rv2969cNMR Structure of the S-Linked Glycopeptide Sublancin 168Immunity to the bacteriocin sublancin 168 Is determined by the SunI (YolF) protein of Bacillus subtilisIdentification of Bacillus subtilis sigma-dependent genes that provide intrinsic resistance to antimicrobial compounds produced by BacilliThe effect of tensile stress on the conformational free energy landscape of disulfide bondsRecombinant pediocin in Lactococcus lactis: increased production by propeptide fusion and improved potency by co-production with PedCDiscovery and in vitro biosynthesis of haloduracin, a two-component lantibiotic.The Rok protein of Bacillus subtilis represses genes for cell surface and extracellular functionsFunctional microdomains in bacterial membranesImproved production of sublancin via introduction of three characteristic promoters into operon clusters responsible for this novel distinct glycopeptide biosynthesisStructure and biosynthesis of a macrocyclic peptide containing an unprecedented lysine-to-tryptophan crosslinkProteomics of protein secretion by Bacillus subtilis: separating the "secrets" of the secretome.Crystal Structure of DsbA from Corynebacterium diphtheriae and Its Functional Implications for CueP in Gram-Positive BacteriaThe phosphoenolpyruvate:sugar phosphotransferase system is involved in sensitivity to the glucosylated bacteriocin sublancin.Expression and crystallization of DsbA from Staphylococcus aureus.Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation.A thiol-disulfide oxidoreductase of the Gram-positive pathogen Corynebacterium diphtheriae is essential for viability, pilus assembly, toxin production and virulence.Ribosomal peptide natural products: bridging the ribosomal and nonribosomal worlds.Applications of thiol-disulfide oxidoreductases for optimized in vivo production of functionally active proteins in BacillusDiversity and applications of Bacillus bacteriocins.The dawning of a 'Golden era' in lantibiotic bioengineering.A disulfide bond-containing alkaline phosphatase triggers a BdbC-dependent secretion stress response in Bacillus subtilisBacillus subtilis StoA Is a thiol-disulfide oxidoreductase important for spore cortex synthesis.Bifunctionality of a biofilm matrix protein controlled by redox state.Disulfide bond formation and cysteine exclusion in gram-positive bacteria.The extracytoplasmic function sigma factor SigY is important for efficient maintenance of the Spβ prophage that encodes sublancin in Bacillus subtilis.The inhibitory spectrum of thermophilin 9 from Streptococcus thermophilus LMD-9 depends on the production of multiple peptides and the activity of BlpG(St), a thiol-disulfide oxidaseFunctional analysis of paralogous thiol-disulfide oxidoreductases in Streptococcus gordonii.Single-peptide DNA-dependent RNA polymerase homologous to multi-subunit RNA polymeraseExtracytoplasmic function sigma factors with overlapping promoter specificity regulate sublancin production in Bacillus subtilis.The large mechanosensitive channel MscL determines bacterial susceptibility to the bacteriocin sublancin 168The two CcdA proteins of Bacillus anthracis differentially affect virulence gene expression and sporulation.Modulation of thiol-disulfide oxidoreductases for increased production of disulfide-bond-containing proteins in Bacillus subtilis.Disulfide Bonds: A Key Modification in Bacterial Extracytoplasmic Proteins.Structure-Activity Relationships of the S-Linked Glycocin Sublancin.Molecular Basis for Specificity of the Extracytoplasmic Thioredoxin ResA
P2860
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P2860
Thiol-disulfide oxidoreductases are essential for the production of the lantibiotic sublancin 168.
description
2002 nî lūn-bûn
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2002 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Thiol-disulfide oxidoreductase ...... the lantibiotic sublancin 168.
@ast
Thiol-disulfide oxidoreductase ...... the lantibiotic sublancin 168.
@en
type
label
Thiol-disulfide oxidoreductase ...... the lantibiotic sublancin 168.
@ast
Thiol-disulfide oxidoreductase ...... the lantibiotic sublancin 168.
@en
prefLabel
Thiol-disulfide oxidoreductase ...... the lantibiotic sublancin 168.
@ast
Thiol-disulfide oxidoreductase ...... the lantibiotic sublancin 168.
@en
P2093
P356
P1476
Thiol-disulfide oxidoreductase ...... the lantibiotic sublancin 168
@en
P2093
Jan Maarten Van Dijl
Jorrit Kabel
Ronald Dorenbos
Sierd Bron
Torsten Stein
Wim J Quax
P304
16682-16688
P356
10.1074/JBC.M201158200
P407
P577
2002-02-28T00:00:00Z