Literature DB >> 17956229

The twin-arginine transport system: moving folded proteins across membranes.

F Sargent1.   

Abstract

The Tat (twin-arginine transport) pathway is a protein-targeting system dedicated to the transmembrane translocation of fully folded proteins. This system is highly prevalent in the cytoplasmic membranes of bacteria and archaea, and is also found in the thylakoid membranes of plant chloroplasts and possibly also in the inner membrane of plant mitochondria. Proteins are targeted to a membrane-embedded Tat translocase by specialized N-terminal twin-arginine signal peptides bearing an SRRXFLK amino acid motif. The genes encoding components of the Tat translocase were discovered approx. 10 years ago, and, since then, research in this area has expanded on a global scale. In this review, the key discoveries in this field are summarized, and recent studies of bacterial twin-arginine signal-peptide-binding proteins are discussed.

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Year:  2007        PMID: 17956229     DOI: 10.1042/BST0350835

Source DB:  PubMed          Journal:  Biochem Soc Trans        ISSN: 0300-5127            Impact factor:   5.407


  46 in total

1.  The physiological opportunism of Desulfitobacterium hafniense strain TCE1 towards organohalide respiration with tetrachloroethene.

Authors:  Aurélie Duret; Christof Holliger; Julien Maillard
Journal:  Appl Environ Microbiol       Date:  2012-06-22       Impact factor: 4.792

Review 2.  Protein export systems of Mycobacterium tuberculosis: novel targets for drug development?

Authors:  Meghan E Feltcher; Jonathan Tabb Sullivan; Miriam Braunstein
Journal:  Future Microbiol       Date:  2010-10       Impact factor: 3.165

3.  Kinetics of precursor interactions with the bacterial Tat translocase detected by real-time FRET.

Authors:  Neal Whitaker; Umesh K Bageshwar; Siegfried M Musser
Journal:  J Biol Chem       Date:  2012-02-07       Impact factor: 5.157

4.  TatD is a central component of a Tat translocon-initiated quality control system for exported FeS proteins in Escherichia coli.

Authors:  Cristina F R O Matos; Alessandra Di Cola; Colin Robinson
Journal:  EMBO Rep       Date:  2009-04-03       Impact factor: 8.807

5.  The Tat system proofreads FeS protein substrates and directly initiates the disposal of rejected molecules.

Authors:  Cristina F R O Matos; Colin Robinson; Alessandra Di Cola
Journal:  EMBO J       Date:  2008-07-10       Impact factor: 11.598

6.  Structure of the twin-arginine signal-binding protein DmsD from Escherichia coli.

Authors:  Suresh Kumar Ramasamy; William M Clemons
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2009-07-21

7.  A stromal pool of TatA promotes Tat-dependent protein transport across the thylakoid membrane.

Authors:  Stefan Frielingsdorf; Mario Jakob; Ralf Bernd Klösgen
Journal:  J Biol Chem       Date:  2008-10-07       Impact factor: 5.157

Review 8.  Protein transport across and into cell membranes in bacteria and archaea.

Authors:  Jijun Yuan; Jessica C Zweers; Jan Maarten van Dijl; Ross E Dalbey
Journal:  Cell Mol Life Sci       Date:  2009-10-10       Impact factor: 9.261

9.  Membrane localization of small proteins in Escherichia coli.

Authors:  Fanette Fontaine; Ryan T Fuchs; Gisela Storz
Journal:  J Biol Chem       Date:  2011-07-21       Impact factor: 5.157

10.  Single-cell, real-time detection of oxidative stress induced in Escherichia coli by the antimicrobial peptide CM15.

Authors:  Heejun Choi; Zhilin Yang; James C Weisshaar
Journal:  Proc Natl Acad Sci U S A       Date:  2015-01-05       Impact factor: 11.205

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