Membrane topology of the Bacillus subtilis pro-sigma(K) processing complex
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The Bacillus subtilis signaling protein SpoIVB defines a new family of serine peptidasesBofA protein inhibits intramembrane proteolysis of pro-sigmaK in an intercompartmental signaling pathway during Bacillus subtilis sporulation.Substrate requirements for regulated intramembrane proteolysis of Bacillus subtilis pro-sigmaKProteolysis of SpolVB is a critical determinant in signalling of Pro-sigmaK processing in Bacillus subtilis.The PDZ domain of the SpoIVB serine peptidase facilitates multiple functions.Evidence that SpoIVFB is a novel type of membrane metalloprotease governing intercompartmental communication during Bacillus subtilis sporulationRapid topology mapping of Escherichia coli inner-membrane proteins by prediction and PhoA/GFP fusion analysisEvidence that subcellular localization of a bacterial membrane protein is achieved by diffusion and capture.Genome-wide dynamic transcriptional profiling in Clostridium beijerinckii NCIMB 8052 using single-nucleotide resolution RNA-SeqScreening of a Leptospira biflexa mutant library to identify genes involved in ethidium bromide tolerance.Forespore signaling is necessary for pro-sigmaK processing during Bacillus subtilis sporulation despite the loss of SpoIVFA upon translational arrestA sporulation membrane protein tethers the pro-sigmaK processing enzyme to its inhibitor and dictates its subcellular localizationProteins Related to the Type I Secretion System Are Associated with Secondary SecA_DEAD Domain Proteins in Some Species of Planctomycetes, Verrucomicrobia, Proteobacteria, Nitrospirae and ChlorobiCompartmentalization of gene expression during Bacillus subtilis spore formation.A second PDZ-containing serine protease contributes to activation of the sporulation transcription factor sigmaK in Bacillus subtilisComplex Formed between Intramembrane Metalloprotease SpoIVFB and Its Substrate, Pro-σKFeatures of Pro-σK important for cleavage by SpoIVFB, an intramembrane metalloprotease.Processing of a membrane protein required for cell-to-cell signaling during endospore formation in Bacillus subtilis.Biochemical and structural insights into intramembrane metalloprotease mechanisms.Residues in conserved loops of intramembrane metalloprotease SpoIVFB interact with residues near the cleavage site in pro-σKStructure and mechanism of intramembrane protease.Function of site-2 proteases in bacteria and bacterial pathogens.Membrane topology of the acyl-lipid desaturase from Bacillus subtilis.Site-2 protease regulated intramembrane proteolysis: sequence homologs suggest an ancient signaling cascade.Effects of supplementary butyrate on butanol production and the metabolic switch in Clostridium beijerinckii NCIMB 8052: genome-wide transcriptional analysis with RNA-Seq.Serine proteases from two cell types target different components of a complex that governs regulated intramembrane proteolysis of pro-sigmaK during Bacillus subtilis development.Interaction of intramembrane metalloprotease SpoIVFB with substrate Pro-σK.Subcellular localization of a sporulation membrane protein is achieved through a network of interactions along and across the septum.Bacillus subtilis Intramembrane Protease RasP Activity in Escherichia coli and In Vitro.The Structure of Bypass of Forespore C, an Intercompartmental Signaling Factor during Sporulation inBacillus
P2860
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P2860
Membrane topology of the Bacillus subtilis pro-sigma(K) processing complex
description
2000 nî lūn-bûn
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2000年の論文
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2000年学术文章
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2000年学术文章
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2000年学术文章
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name
Membrane topology of the Bacillus subtilis pro-sigma
@nl
Membrane topology of the Bacillus subtilis pro-sigma(K) processing complex
@en
type
label
Membrane topology of the Bacillus subtilis pro-sigma
@nl
Membrane topology of the Bacillus subtilis pro-sigma(K) processing complex
@en
prefLabel
Membrane topology of the Bacillus subtilis pro-sigma
@nl
Membrane topology of the Bacillus subtilis pro-sigma(K) processing complex
@en
P2860
P1476
Membrane topology of the Bacillus subtilis pro-sigma(K) processing complex
@en
P2093
P2860
P304
P356
10.1128/JB.182.2.278-285.2000
P407
P577
2000-01-01T00:00:00Z