ArticleThe Journal of biological chemistry2010
Subunit organization in the TatA complex of the twin arginine protein translocase: a site-directed EPR spin labeling study.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed, 29 citations in OpenAlex.
- Structural Dynamics and Topology of the Inactive Form of SThe journal of physical chemistry. B · 2020Article
- Continuous Wave Electron Paramagnetic Resonance Spectroscopy Reveals the Structural Topology and Dynamic Properties of Active Pinholin SThe journal of physical chemistry. B · 2019Article
- Transport of Folded Proteins by the Tat System.The protein journal · 2019Review
- The Twin-Arginine Pathway for Protein Secretion.EcoSal Plus · 2019Review
- Structural basis for TatA oligomerization: an NMR study of Escherichia coli TatA dimeric structure.PloS one · 2014Article
- Quantification of free cysteines in membrane and soluble proteins using a fluorescent dye and thermal unfolding.Nature protocols · 2013Article
- Structural model for the protein-translocating element of the twin-arginine transport system.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Substrate-dependent assembly of the Tat translocase as observed in live Escherichia coli cells.PloS one · 2013Article
- Identification and evaluation of twin-arginine translocase inhibitors.Antimicrobial agents and chemotherapy · 2012Article
- The twin-arginine translocation (Tat) protein export pathway.Nature reviews. Microbiology · 2012Review
- Twin-arginine-dependent translocation of folded proteins.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Mapping precursor-binding site on TatC subunit of twin arginine-specific protein translocase by site-specific photo cross-linking.The Journal of biological chemistry · 2012Article
- Transmembrane insertion of twin-arginine signal peptides is driven by TatC and regulated by TatB.Nature communications · 2012Article
- Early contacts between substrate proteins and TatA translocase component in twin-arginine translocation.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The Tat system is used to transport folded proteins across the cytoplasmic membrane in bacteria and archaea and across the thylakoid membrane of plant chloroplasts. Multimers of the integral membrane TatA protein are thought to form the protein-conducting element of the Tat pathway. Nitroxide radicals were introduced at selected positions within the transmembrane helix of Escherichia coli TatA and used to probe the structure of detergent-solubilized TatA complexes by EPR spectroscopy. A comparison of spin label mobilities allowed classification of individual residues as buried within the TatA complex or exposed at the surface and suggested that residues Ile(12) and Val(14) are involved in interactions between helices. Analysis of inter-spin distances suggested that the transmembrane helices of TatA subunits are arranged as a single-walled ring containing a contact interface between Ile(12) on one subunit and Val(14) on an adjacent subunit. Experiments in which labeled and unlabeled TatA samples were mixed demonstrate that TatA subunits are exchanged between TatA complexes. This observation is consistent with the TatA dynamic polymerization model for the mechanism of Tat transport.
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Registered trials
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