Solution NMR structure of the TatA component of the twin-arginine protein transport system from gram-positive bacterium Bacillus subtilis
about
Channel crossing: how are proteins shipped across the bacterial plasma membrane?A microbial sensor for discovering structural probes of protein misfolding and aggregationSubstrate-dependent assembly of the Tat translocase as observed in live Escherichia coli cellsStructure of the TatC core of the twin-arginine protein transport systemStructural model for the protein-translocating element of the twin-arginine transport systemConserved Signal Peptide Recognition Systems across the Prokaryotic DomainsStructural Basis for TatA Oligomerization: An NMR Study of Escherichia coli TatA Dimeric StructureSecretome of obligate intracellular Rickettsia.Towards understanding the Tat translocation mechanism through structural and biophysical studies of the amphipathic region of TatA from Escherichia coli.The chloroplast twin arginine transport (Tat) component, Tha4, undergoes conformational changes leading to Tat protein transport.Investigating the interaction between peptides of the amphipathic helix of Hcf106 and the phospholipid bilayer by solid-state NMR spectroscopy.Substrate-gated docking of pore subunit Tha4 in the TatC cavity initiates Tat translocase assembly.Twin-arginine-dependent translocation of folded proteins.The twin-arginine translocation (Tat) protein export pathway.Mechanistic Aspects of Folded Protein Transport by the Twin Arginine Translocase (Tat).Ultrastructural characterisation of Bacillus subtilis TatA complexes suggests they are too small to form homooligomeric translocation pores.Twin-Arginine Protein Translocation.Assembling the Tat protein translocase.Salt sensitivity of minimal twin arginine translocases.Early contacts between substrate proteins and TatA translocase component in twin-arginine translocation.Substrate-triggered position switching of TatA and TatB during Tat transport in Escherichia coli.In vivo experiments do not support the charge zipper model for Tat translocase assemblyStructure of TatA paralog, TatE, suggests a structurally homogeneous form of Tat protein translocase that transports folded proteins of differing diameter.Transmembrane insertion of twin-arginine signal peptides is driven by TatC and regulated by TatB.Escherichia coli TatA and TatB proteins have N-out, C-in topology in intact cells.The Tat system for membrane translocation of folded proteins recruits the membrane-stabilizing Psp machinery in Escherichia coli.Molecular dissection of TatC defines critical regions essential for protein transport and a TatB-TatC contact site.Expression of the bifunctional Bacillus subtilis TatAd protein in Escherichia coli reveals distinct TatA/B-family and TatB-specific domains.Structural features of the TatC membrane protein that determine docking and insertion of a twin-arginine signal peptide.Unanticipated functional diversity among the TatA-type components of the Tat protein translocase.Functional Analysis of the Minimal Twin-Arginine Translocation System Components from Streptococcus thermophilus CGMCC 7.179 in Escherichia coli DE3.
P2860
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P2860
Solution NMR structure of the TatA component of the twin-arginine protein transport system from gram-positive bacterium Bacillus subtilis
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2010 nî lūn-bûn
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2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
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2010 թվականի նոյեմբերին հրատարակված գիտական հոդված
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2010年の論文
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2010年論文
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2010年論文
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2010年論文
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2010年論文
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2010年論文
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2010年论文
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name
Solution NMR structure of the ...... ve bacterium Bacillus subtilis
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Solution NMR structure of the ...... ve bacterium Bacillus subtilis
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Solution NMR structure of the ...... ve bacterium Bacillus subtilis
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Solution NMR structure of the ...... ve bacterium Bacillus subtilis
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Solution NMR structure of the ...... ve bacterium Bacillus subtilis
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Solution NMR structure of the ...... ve bacterium Bacillus subtilis
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Solution NMR structure of the ...... ve bacterium Bacillus subtilis
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Solution NMR structure of the ...... ve bacterium Bacillus subtilis
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Solution NMR structure of the ...... ve bacterium Bacillus subtilis
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P2093
P356
P1476
Solution NMR structure of the ...... ve bacterium Bacillus subtilis
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P2093
P304
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10.1021/JA1053785
P407
P50
P577
2010-11-17T00:00:00Z