Literature DB >> 23422074

Effect of cargo size and shape on the transport efficiency of the bacterial Tat translocase.

Neal Whitaker1, Umesh Bageshwar, Siegfried M Musser.   

Abstract

The Tat machinery translocates fully-folded and oligomeric substrates. The passage of large, bulky cargos across an ion-tight membrane suggests the need to match pore and cargo size, and therefore that Tat transport efficiency may depend on both cargo size and shape. A series of cargos of different sizes and shapes were generated using the natural Tat substrate pre-SufI as a base. Four (of 17) cargos transported with significant (>20% of wild-type) efficiencies. These results indicate that cargo size and shape significantly influence Tat transportability.
Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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Year:  2013        PMID: 23422074      PMCID: PMC3613985          DOI: 10.1016/j.febslet.2013.02.015

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  22 in total

1.  Characterization of the early steps of OE17 precursor transport by the thylakoid DeltapH/Tat machinery.

Authors:  S M Musser; S M Theg
Journal:  Eur J Biochem       Date:  2000-05

2.  Co-translocation of a periplasmic enzyme complex by a hitchhiker mechanism through the bacterial tat pathway.

Authors:  A Rodrigue; A Chanal; K Beck; M Müller; L F Wu
Journal:  J Biol Chem       Date:  1999-05-07       Impact factor: 5.157

3.  Membrane interactions and self-association of the TatA and TatB components of the twin-arginine translocation pathway.

Authors:  E De Leeuw; I Porcelli; F Sargent; T Palmer; B C Berks
Journal:  FEBS Lett       Date:  2001-10-05       Impact factor: 4.124

4.  Model energy landscapes and the force-induced dissociation of ligand-receptor bonds.

Authors:  T Strunz; K Oroszlan; I Schumakovitch; H Güntherodt; M Hegner
Journal:  Biophys J       Date:  2000-09       Impact factor: 4.033

5.  Energetics of protein transport across biological membranes. a study of the thylakoid DeltapH-dependent/cpTat pathway.

Authors:  Nathan N Alder; Steven M Theg
Journal:  Cell       Date:  2003-01-24       Impact factor: 41.582

6.  Twin-arginine translocase mutations that suppress folding quality control and permit export of misfolded substrate proteins.

Authors:  Mark A Rocco; Dujduan Waraho-Zhmayev; Matthew P DeLisa
Journal:  Proc Natl Acad Sci U S A       Date:  2012-07-30       Impact factor: 11.205

Review 7.  Recombinant protein secretion in Escherichia coli.

Authors:  F J M Mergulhão; D K Summers; G A Monteiro
Journal:  Biotechnol Adv       Date:  2005-01-08       Impact factor: 14.227

8.  A folded protein can be transported across the chloroplast envelope and thylakoid membranes.

Authors:  S A Clark; S M Theg
Journal:  Mol Biol Cell       Date:  1997-05       Impact factor: 4.138

Review 9.  Export of complex cofactor-containing proteins by the bacterial Tat pathway.

Authors:  Tracy Palmer; Frank Sargent; Ben C Berks
Journal:  Trends Microbiol       Date:  2005-04       Impact factor: 17.079

10.  The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter.

Authors:  Ulrich Gohlke; Lee Pullan; Christopher A McDevitt; Ida Porcelli; Erik de Leeuw; Tracy Palmer; Helen R Saibil; Ben C Berks
Journal:  Proc Natl Acad Sci U S A       Date:  2005-07-18       Impact factor: 11.205

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  1 in total

1.  Oligomerization state of the functional bacterial twin-arginine translocation (Tat) receptor complex.

Authors:  Ankith Sharma; Rajdeep Chowdhury; Siegfried M Musser
Journal:  Commun Biol       Date:  2022-09-19
  1 in total

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