Mapping the Signal Peptide Binding and Oligomer Contact Sites of the Core Subunit of the Pea Twin Arginine Protein Translocase[W]

No abstract is available for this paper.

• Publication year

  2013

• Venue

  The Plant Cell

• Publication date

  2013-03-01

• Fields of study

  Biology, Medicine, Chemistry, Environmental Science

• Identifiers
  DOI 10.1105/tpc.112.107409PMID 23512851PMCID PMC3634702
• 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.

• Intra-plastid protein trafficking: how plant cells adapted prokaryotic mechanisms to the eukaryotic condition.

  2013cited by this paper
• Stoichiometry for binding and transport by the twin arginine translocation system

  2012cited by this paper
• Molecular dissection of TatC defines critical regions essential for protein transport and a TatB–TatC contact site

  2012influential reference
• Structure of the TatC core of the twin-arginine protein transport system

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

  2012influential reference
• Twin-arginine-dependent translocation of folded proteins

  2012cited by this paper
• The twin-arginine translocation (Tat) protein export pathway

  2012cited by this paper
• Early Contacts between Substrate Proteins and TatA Translocase Component in Twin-arginine Translocation*

  2011cited by this paper
• TatB Functions as an Oligomeric Binding Site for Folded Tat Precursor Proteins

  2010cited by this paper
• Multiple precursor proteins bind individual Tat receptor complexes and are collectively transported

  2010cited by this paper
• Plastids Contain a Second Sec Translocase System with Essential Functions1[W][OA]

  2010cited by this paper
• Localization and integration of thylakoid protein translocase subunit cpTatC.

  2009cited by this paper
• Clustering of C-terminal stromal domains of Tha4 homo-oligomers during translocation by the Tat protein transport system.

  2009cited by this paper
• Predicting the effects of coding non-synonymous variants on protein function using the SIFT algorithm

  2009cited by this paper
• Variable stoichiometry of the TatA component of the twin-arginine protein transport system observed by in vivo single-molecule imaging

  2008cited by this paper
• Plastid protein import and sorting: different paths to the same compartments.

  2008cited by this paper
• Evidence for a dynamic and transient pathway through the TAT protein transport machinery

  2007cited by this paper
• The Thylakoid Proton Gradient Promotes an Advanced Stage of Signal Peptide Binding Deep within the Tat Pathway Receptor Complex*

  2007cited by this paper
• 18 - The Sec and Tat Protein Translocation Pathways in Chloroplasts

  2007cited by this paper
• The entire N-terminal half of TatC is involved in twin-arginine precursor binding.

  2007influential reference
• TatBC, TatB, and TatC form structurally autonomous units within the twin arginine protein transport system of Escherichia coli

  2007influential reference
• Cysteine Scanning Mutagenesis and Topological Mapping of the Escherichia coli Twin-Arginine Translocase TatC Component

  2007cited by this paper
• The TatBC complex formation suppresses a modular TatB‐multimerization in Escherichia coli

  2007influential reference
• Subunit composition and in vivo substrate‐binding characteristics of Escherichia coli Tat protein complexes expressed at native levels

  2006cited by this paper
• The Function and Diversity of Plastid Protein Import Pathways: A Multilane GTPase Highway into Plastids

  2006cited by this paper
• Efficient Twin Arginine Translocation (Tat) Pathway Transport of a Precursor Protein Covalently Anchored to Its Initial cpTatC Binding Site*

  2006cited by this paper
• Oligomers of Tha4 Organize at the Thylakoid Tat Translocase during Protein Transport*

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

  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.

  2005influential reference
• New Functions of the Thylakoid Membrane Proteome of Arabidopsis thaliana Revealed by a Simple, Fast, and Versatile Fractionation Strategy*

  2004cited by this paper
• UCSF Chimera—A visualization system for exploratory research and analysis

  2004influential reference
• Requirement of a Tha4-conserved Transmembrane Glutamate in Thylakoid Tat Translocase Assembly Revealed by Biochemical Complementation*

  2003cited by this paper
• An alternative model of the twin arginine translocation system.

  2003cited by this paper
• Functional assembly of thylakoid deltapH-dependent/Tat protein transport pathway components in vitro.

  2003cited by this paper
• Light-Harvesting Antennas in Photosynthesis

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

  2003influential reference
• SIFT: predicting amino acid changes that affect protein function

  2003cited by this paper
• Biogenesis of Green Plant Thylakoid Membranes

  2003cited by this paper
• Protein translocons: multifunctional mediators of protein translocation across membranes.

  2003cited by this paper
• A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid ΔpH/Tat translocase

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

  2002influential reference
• Essential Cytoplasmic Domains in the Escherichia coli TatC Protein*

  2002cited by this paper
• Proteome Map of the Chloroplast Lumen of Arabidopsis thaliana *

  2002cited by this paper
• Post-translational protein translocation into thylakoids by the Sec and DeltapH-dependent pathways.

  2001cited by this paper
• An essential role of a TatC homologue of a ΔpH- dependent protein transporter in thylakoid membrane formation during chloroplast development in Arabidopsis thaliana

  2001cited by this paper
• Predicting deleterious amino acid substitutions.

  2001cited by this paper
• Chloroplast TatC plays a direct role in thylakoid ΔpH‐dependent protein transport

  2001cited by this paper
• Chloroplast TatC plays a direct role in thylakoid (Delta)pH-dependent protein transport.

  2001cited by this paper
• Thylakoid ΔpH-dependent precursor proteins bind to a cpTatC–Hcf106 complex before Tha4-dependent transport

  2001cited by this paper
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  1986cited by this paper
• COPPER ENZYMES IN ISOLATED CHLOROPLASTS. POLYPHENOLOXIDASE IN BETA VULGARIS.

  1949cited by this paper

• New insights into the Tat protein transport cycle from characterizing the assembled Tat translocon

  2022cites this paper
• Insights into substrate-mediated assembly of the chloroplast TAT receptor complex

  2020influential citation
• Liquid-Liquid Phase Transition Drives Intra-chloroplast Cargo Sorting.

  2020cites this paper
• Analysis of haloarchaeal twin-arginine translocase pathway reveals the diversity of the machineries

  2019cites this paper
• Surface-exposed domains of TatB involved in the structural and functional assembly of the Tat translocase in Escherichia coli

  2019cites this paper
• Precursor–Receptor Interactions in the Twin Arginine Protein Transport Pathway Probed with a New Receptor Complex Preparation

  2018cites this paper
• Unanticipated functional diversity among the TatA-type components of the Tat protein translocase

  2018cites this paper
• The Tat protein transport system: intriguing questions and conundrums.

  2018cites this paper
• Thylakoid-integrated recombinant Hcf106 participates in the chloroplast Twin Arginine Transport (cpTat) system

  2018influential citation
• Routing of thylakoid lumen proteins by the chloroplast twin arginine transport pathway

  2018cites this paper
• 1 Thylakoid-integrated recombinant Hcf 106 participates in the chloroplast Twin 1 Arginine Transport ( cpTat ) system 2 3

  2018cites this paper
• Thylakoid‐integrated recombinant Hcf106 participates in the chloroplast twin arginine transport system†

  2018cites this paper
• Structural features of the TatC membrane protein that determine docking and insertion of a twin-arginine signal peptide

  2017influential citation
• A Hinged Signal Peptide Hairpin Enables Tat-Dependent Protein Translocation.

  2017cites this paper
• Evaluating a New High-throughput Twin-Arginine Translocase Assay in Bacteria for Therapeutic Applications

  2017cites this paper
• Signal Peptide Hydrophobicity Modulates Interaction with the Twin-Arginine Translocase

  2017cites this paper
• Proofreading of substrate by the Escherichia coli Twin Arginine Translocase

  2017cites this paper
• A signal sequence suppressor mutant that stabilizes an assembled state of the twin arginine translocase

  2017cites this paper
• Assembling the Tat protein translocase

  2016influential citation
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  2016cites this paper
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• TatA complexes exhibit a marked change in organisation in response to expression of the TatBC complex

  2016cites this paper
• Mapping protein-protein interactions in the Escherichia coli twin arginine translocase

  2016cites this paper
• FUNCTIONAL INTERACTION ANALYSIS OF CHLOROPLAST TWIN ARGININE TRANSLOCATION (CPTAT) PATHWAY AND ITS ROLE IN PLASTID DEVELOPMENT

  2016cites this paper
• Mechanistic Aspects of Folded Protein Transport by the Twin Arginine Translocase (Tat)*

  2015influential citation
• The TatC component of the twin‐arginine protein translocase functions as an obligate oligomer

  2015cites this paper
• The twin-arginine protein translocation pathway.

  2015cites this paper
• TatE as a Regular Constituent of Bacterial Twin-arginine Protein Translocases*

  2015cites this paper
• Initial assembly steps of a translocase for folded proteins

  2015cites this paper
• An investigation into the structure and localisation of the bacterial twin arginine translocase (Tat) complexes by electron microscopy

  2015cites this paper
• The TatBC complex of the Tat protein translocase in Escherichia coli and its transition to the substrate-bound TatABC complex.

  2014cites this paper
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  2014cites this paper
• Protein Routing Processes in the Thylakoid

  2014cites this paper
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  2014cites this paper
• Substrate-gated docking of pore subunit Tha4 in the TatC cavity initiates Tat translocase assembly

  2014cites this paper
• Structural biology of Tat protein transport.

  2014cites this paper
• Substrate-Dependent Assembly of the Tat Translocase as Observed in Live Escherichia coli Cells

  2013cites this paper
• Solid-state NMR investigations of peptide-lipid interactions of the transmembrane domain of a plant-derived protein, Hcf106.

  2013cites this paper
• Live cell imaging shows reversible assembly of the TatA component of the twin-arginine protein transport system

  2013cites this paper
• Special Delivery: In Vitro Functional Examination of the Twin-Arginine Transport Complex Core Component cpTatC

  2013cites this paper