Literature DB >> 25494301

The twin-arginine protein translocation pathway.

Ben C Berks1.   

Abstract

The twin-arginine translocation (Tat) system, found in prokaryotes, chloroplasts, and some mitochondria, allows folded proteins to be moved across membranes. How this transport is achieved without significant ion leakage is an intriguing mechanistic question. Tat transport is mediated by complexes formed from small integral membrane proteins from just two protein families. Atomic-resolution structures have recently been determined for representatives of both these protein families, providing the first molecular-level glimpse of the Tat machinery. I review our current understanding of the mechanism of Tat transport in light of these new structural data.

Entities:  

Keywords:  bacterial protein export; membrane protein; protein transport; signal peptide; thylakoid import; twin-arginine

Mesh:

Substances:

Year:  2014        PMID: 25494301     DOI: 10.1146/annurev-biochem-060614-034251

Source DB:  PubMed          Journal:  Annu Rev Biochem        ISSN: 0066-4154            Impact factor:   23.643


  59 in total

1.  Evaluating a New High-throughput Twin-Arginine Translocase Assay in Bacteria for Therapeutic Applications.

Authors:  Deepanjan Ghosh; Shridhar Chougule; Vellore Sunder Avinash; Sureshkumar Ramasamy
Journal:  Curr Microbiol       Date:  2017-08-04       Impact factor: 2.188

Review 2.  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

Review 3.  The Principles of Protein Targeting and Transport Across Cell Membranes.

Authors:  Yuanyuan Chen; Sri Karthika Shanmugam; Ross E Dalbey
Journal:  Protein J       Date:  2019-06       Impact factor: 2.371

Review 4.  Expanding Role of Type II Secretion in Bacterial Pathogenesis and Beyond.

Authors:  Nicholas P Cianciotto; Richard C White
Journal:  Infect Immun       Date:  2017-04-21       Impact factor: 3.441

5.  The Tat Substrate SufI Is Critical for the Ability of Yersinia pseudotuberculosis To Cause Systemic Infection.

Authors:  Ummehan Avican; Tugrul Doruk; Yngve Östberg; Anna Fahlgren; Åke Forsberg
Journal:  Infect Immun       Date:  2017-03-23       Impact factor: 3.441

Review 6.  The Tat protein transport system: intriguing questions and conundrums.

Authors:  Shruthi Hamsanathan; Siegfried M Musser
Journal:  FEMS Microbiol Lett       Date:  2018-06-01       Impact factor: 2.742

Review 7.  Routing of thylakoid lumen proteins by the chloroplast twin arginine transport pathway.

Authors:  Christopher Paul New; Qianqian Ma; Carole Dabney-Smith
Journal:  Photosynth Res       Date:  2018-08-12       Impact factor: 3.573

8.  ArtA-Dependent Processing of a Tat Substrate Containing a Conserved Tripartite Structure That Is Not Localized at the C Terminus.

Authors:  Mohd Farid Abdul Halim; Jonathan D Stoltzfus; Stefan Schulze; Micheal Hippler; Mechthild Pohlschroder
Journal:  J Bacteriol       Date:  2017-03-14       Impact factor: 3.490

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.  Bacterial N-Glycosylation Efficiency Is Dependent on the Structural Context of Target Sequons.

Authors:  Julie Michelle Silverman; Barbara Imperiali
Journal:  J Biol Chem       Date:  2016-08-29       Impact factor: 5.157

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.