Structural diversity in twin-arginine signal peptide-binding proteins
about
The transcriptionally active regions in the genome of Bacillus subtilisStructural Analysis of a Monomeric Form of the Twin-Arginine Leader Peptide Binding Chaperone Escherichia coli DmsDConserved Signal Peptide Recognition Systems across the Prokaryotic DomainsNitrate and periplasmic nitrate reductasesA stromal pool of TatA promotes Tat-dependent protein transport across the thylakoid membrane.Features of a twin-arginine signal peptide required for recognition by a Tat proofreading chaperone.The mononuclear molybdenum enzymes.It takes two to tango: two TatA paralogues and two redox enzyme-specific chaperones are involved in the localization of twin-arginine translocase substrates in Campylobacter jejuni.Physiological and evolutionary studies of NAP systems in Shewanella piezotolerans WP3.NarJ subfamily system specific chaperone diversity and evolution is directed by respiratory enzyme associationsInterconvertibility of lipid- and translocon-bound forms of the bacterial Tat precursor pre-SufI.The twin-arginine translocation system: contributions to the pathobiology of Campylobacter jejuni.The twin-arginine translocation (Tat) protein export pathway.The role of FeS clusters for molybdenum cofactor biosynthesis and molybdoenzymes in bacteria.Nitrate reduction in Haloferax alexandrinus: the case of assimilatory nitrate reductase.The twin-arginine signal peptide of Bacillus subtilis YwbN can direct either Tat- or Sec-dependent secretion of different cargo proteins: secretion of active subtilisin via the B. subtilis Tat pathway.High-salinity growth conditions promote Tat-independent secretion of Tat substrates in Bacillus subtilis.Transposon and deletion mutagenesis of genes involved in perchlorate reduction in Azospira suillum PSCharacterization of a periplasmic nitrate reductase in complex with its biosynthetic chaperone.Multifaceted SlyD from Helicobacter pylori: implication in [NiFe] hydrogenase maturation.The hydrophobic region of the DmsA twin-arginine leader peptide determines specificity with chaperone DmsD.Overlapping transport and chaperone-binding functions within a bacterial twin-arginine signal peptide.Differential Interactions between Tat-specific redox enzyme peptides and their chaperones.Intrinsic GTPase activity of a bacterial twin-arginine translocation proofreading chaperone induced by domain swapping.A regulatory domain controls the transport activity of a twin-arginine signal peptide.Reduction of nitrate in Shewanella oneidensis depends on atypical NAP and NRF systems with NapB as a preferred electron transport protein from CymA to NapA.Basis of recognition between the NarJ chaperone and the N-terminus of the NarG subunit from Escherichia coli nitrate reductase.
P2860
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P2860
Structural diversity in twin-arginine signal peptide-binding proteins
description
2007 nî lūn-bûn
@nan
2007 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Structural diversity in twin-arginine signal peptide-binding proteins
@ast
Structural diversity in twin-arginine signal peptide-binding proteins
@en
Structural diversity in twin-arginine signal peptide-binding proteins
@nl
type
label
Structural diversity in twin-arginine signal peptide-binding proteins
@ast
Structural diversity in twin-arginine signal peptide-binding proteins
@en
Structural diversity in twin-arginine signal peptide-binding proteins
@nl
prefLabel
Structural diversity in twin-arginine signal peptide-binding proteins
@ast
Structural diversity in twin-arginine signal peptide-binding proteins
@en
Structural diversity in twin-arginine signal peptide-binding proteins
@nl
P2093
P2860
P50
P356
P1476
Structural diversity in twin-arginine signal peptide-binding proteins
@en
P2093
Chris A E M Spronk
Grant Buchanan
Verity Lyall
P2860
P304
P356
10.1073/PNAS.0703967104
P407
P577
2007-10-02T00:00:00Z