The glove-like structure of the conserved membrane protein TatC provides insight into signal sequence recognition in twin-arginine translocation.

No abstract is available for this paper.

• Publication year

  2013

• Venue

  Structure

• Publication date

  2013-05-07

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/j.str.2013.03.004PMID 23583035PMCID PMC3653977
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• The twin-arginine translocation (Tat) protein export pathway

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• Genetic Evidence for a Tight Cooperation of TatB and TatC during Productive Recognition of Twin-Arginine (Tat) Signal Peptides in Escherichia coli

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• Molecular dissection of TatC defines critical regions essential for protein transport and a TatB–TatC contact site

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• Structure analysis of the membrane-bound PhoD signal peptide of the Tat translocase shows an N-terminal amphiphilic helix.

  2012cited by this paper
• Mapping Precursor-binding Site on TatC Subunit of Twin Arginine-specific Protein Translocase by Site-specific Photo Cross-linking*

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• Transmembrane insertion of twin-arginine signal peptides is driven by TatC and regulated by TatB

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• Structure of the TatC core of the twin-arginine protein transport system

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• Genetic Evidence for a TatC Dimer at the Core of the Escherichia coli Twin Arginine (Tat) Protein Translocase

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• The Pfam protein families database

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  2010cited by this paper
• Super-resolution biomolecular crystallography with low-resolution data

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• Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system

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• Interconvertibility of lipid‐ and translocon‐bound forms of the bacterial Tat precursor pre‐SufI

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• Bioenergetic requirements of a Tat‐dependent substrate in the halophilic archaeon Haloarcula hispanica

  2008cited by this paper
• Following the Path of a Twin-arginine Precursor along the TatABC Translocase of Escherichia coli*

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• Flat-Bottom Strategy for Improved Accuracy in Protein Side-Chain Placements.

  2008cited by this paper
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• The Thylakoid Proton Gradient Promotes an Advanced Stage of Signal Peptide Binding Deep within the Tat Pathway Receptor Complex*

  2007cited by this paper
• Clustal W and Clustal X version 2.0

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• Escherichia coli Twin Arginine (Tat) Mutant Translocases Possessing Relaxed Signal Peptide Recognition Specificities*

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• GPCR Engineering Yields High-Resolution Structural Insights into β2-Adrenergic Receptor Function

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• The entire N-terminal half of TatC is involved in twin-arginine precursor binding.

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• Cysteine Scanning Mutagenesis and Topological Mapping of the Escherichia coli Twin-Arginine Translocase TatC Component

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  2007cited by this paper
• Escherichia coli tatC mutations that suppress defective twin-arginine transporter signal peptides.

  2007cited by this paper
• Evidence for a dynamic and transient pathway through the TAT protein transport machinery

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  2006cited by this paper
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• Cysteine-scanning Mutagenesis and Disulfide Mapping Studies of the Conserved Domain of the Twin-arginine Translocase TatB Component*

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• Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection

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• The tatC gene cluster is essential for viability in halophilic archaea.

  2006cited by this paper
• The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter.

  2005cited by this paper
• Characterisation of Tat protein transport complexes carrying inactivating mutations.

  2005cited by this paper
• Mutations in subunits of the Escherichia coli twin-arginine translocase block function via differing effects on translocation activity or tat complex structure.

  2005cited by this paper
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  2005cited by this paper
• Genetic and Biochemical Analysis of the Twin-Arginine Translocation Pathway in Halophilic Archaea

  2005cited by this paper
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• Evidence for interactions between domains of TatA and TatB from mutagenesis of the TatABC subunits of the twin‐arginine translocase

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  2004cited by this paper
• A periplasmic fluorescent reporter protein and its application in high-throughput membrane protein topology analysis.

  2004cited by this paper
• Topological studies on the twin-arginine translocase component TatC.

  2004cited by this paper
• Langevin dynamics in constant pressure extended systems.

  2004cited by this paper
• A subset of bacterial inner membrane proteins integrated by the twin‐arginine translocase

  2003cited by this paper
• An Escherichia coli twin-arginine signal peptide switches between helical and unstructured conformations depending on the hydrophobicity of the environment.

  2003cited by this paper
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• Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli.

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• Prokaryotic Utilization of the Twin-Arginine Translocation Pathway: a Genomic Survey

  2003cited by this paper
• Essential Cytoplasmic Domains in the Escherichia coli TatC Protein*

  2002cited by this paper
• Protein transport in the halophilic archaeon Halobacterium sp. NRC-1: a major role for the twin-arginine translocation pathway?

  2002cited by this paper
• Functional complexity of the twin‐arginine translocase TatC component revealed by site‐directed mutagenesis

  2002influential reference
• Effects of the twin-arginine translocase on secretion of virulence factors, stress response, and pathogenesis

  2002cited by this paper
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• The trimeric thylakoidal Tat receptor complex consists of a homo-oligomeric TatC core with associated TatB subunits

  2025cites this paper
• The Transmembrane Glutamate Serves as a pH Sensor for Tha4 Oligomerization During Twin Arginine Transport of Proteins

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  2025cites this paper
• The thylakoidal Tat receptor complex appears as a homo-trimeric TatC core with three associated TatB subunits.

  2025cites this paper
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  2024cites this paper
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