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Structural features of the TatC membrane protein that determine docking and insertion of a twin-arginine signal peptide

  • Published:2017-12 Issue:52 Volume:292 Page:21320-21329
  • ISSN:0021-9258
  • Container-title:Journal of Biological Chemistry
  • language:en
  • Short-container-title:Journal of Biological Chemistry

Author:

Blümmel Anne-Sophie,Drepper Friedel,Knapp Bettina,Eimer Ekaterina,Warscheid Bettina,Müller Matthias,Fröbel Julia

Funder

Deutsche Forschungsgemeinschaft

Excellence Initiative of the German Federal and State Governments

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference50 articles.

1. Mechanistic aspects of folded protein transport by the twin-arginine translocase (Tat);Cline;J. Biol. Chem,2015

2. Structural biology of Tat protein transport;Berks;Curr. Opin. Struct. Biol,2014

3. Twin-arginine-dependent translocation of folded proteins;Fröbel;Philos. Trans. R. Soc. Lond. B Biol. Sci,2012

4. The twin-arginine translocation (Tat) protein export pathway;Palmer;Nat. Rev. Microbiol,2012

5. Protein transport by the bacterial Tat pathway;Patel;Biochim. Biophys. Acta,2014
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