Literature DB >> 12608575

An alternative model of the twin arginine translocation system.

Thomas Brüser1, Carsten Sanders.   

Abstract

The twin arginine translocation (Tat) system is a machinery which can translocate folded proteins across energy transducing membranes. Currently it is supposed that Tat substrates bind directly to Tat translocon components before a ApH-driven translocation occurs. In this review, an alternative model is presented which proposes that membrane integration could precede Tat-dependent translocation. This idea is mainly supported by the recent observations of Tat-independent membrane insertion of Tat substrates in vivo and in vitro. Membrane insertion may allow i) a quality control of the folded state by membrane bound proteases like FtsH, ii) the recognition of the membrane spanning signal peptide by Tat system components, and iii) a pulling mechanism of translocation. In some cases of folded Tat substrates, the membrane targeting process may require ATP-dependent N-terminal unfolding-steps.

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Year:  2003        PMID: 12608575     DOI: 10.1078/0944-5013-00176

Source DB:  PubMed          Journal:  Microbiol Res        ISSN: 0944-5013            Impact factor:   5.415


  49 in total

1.  Early contacts between substrate proteins and TatA translocase component in twin-arginine translocation.

Authors:  Julia Fröbel; Patrick Rose; Matthias Müller
Journal:  J Biol Chem       Date:  2011-10-31       Impact factor: 5.157

Review 2.  Twin-arginine-dependent translocation of folded proteins.

Authors:  Julia Fröbel; Patrick Rose; Matthias Müller
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2012-04-19       Impact factor: 6.237

3.  Multiple precursor proteins bind individual Tat receptor complexes and are collectively transported.

Authors:  Xianyue Ma; Kenneth Cline
Journal:  EMBO J       Date:  2010-03-25       Impact factor: 11.598

Review 4.  A little help from my friends: quality control of presecretory proteins in bacteria.

Authors:  Adam C Fisher; Matthew P DeLisa
Journal:  J Bacteriol       Date:  2004-11       Impact factor: 3.490

5.  Clustering of C-terminal stromal domains of Tha4 homo-oligomers during translocation by the Tat protein transport system.

Authors:  Carole Dabney-Smith; Kenneth Cline
Journal:  Mol Biol Cell       Date:  2009-02-04       Impact factor: 4.138

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

Authors:  Anne-Sophie Blümmel; Friedel Drepper; Bettina Knapp; Ekaterina Eimer; Bettina Warscheid; Matthias Müller; Julia Fröbel
Journal:  J Biol Chem       Date:  2017-10-31       Impact factor: 5.157

7.  Following the path of a twin-arginine precursor along the TatABC translocase of Escherichia coli.

Authors:  Sascha Panahandeh; Carlo Maurer; Michael Moser; Matthew P DeLisa; Matthias Müller
Journal:  J Biol Chem       Date:  2008-10-03       Impact factor: 5.157

Review 8.  Mechanistic Aspects of Folded Protein Transport by the Twin Arginine Translocase (Tat).

Authors:  Kenneth Cline
Journal:  J Biol Chem       Date:  2015-05-14       Impact factor: 5.157

9.  The h-region of twin-arginine signal peptides supports productive binding of bacterial Tat precursor proteins to the TatBC receptor complex.

Authors:  Agnes Ulfig; Julia Fröbel; Frank Lausberg; Anne-Sophie Blümmel; Anna Katharina Heide; Matthias Müller; Roland Freudl
Journal:  J Biol Chem       Date:  2017-05-17       Impact factor: 5.157

10.  TatB functions as an oligomeric binding site for folded Tat precursor proteins.

Authors:  Carlo Maurer; Sascha Panahandeh; Anna-Carina Jungkamp; Michael Moser; Matthias Müller
Journal:  Mol Biol Cell       Date:  2010-10-06       Impact factor: 4.138

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