The twin-arginine translocation (Tat) system

Tracy Palmer; Ben C Berks

doi:10.1016/j.cub.2024.02.039

The twin-arginine translocation (Tat) system

Curr Biol. 2024 Apr 8;34(7):R267-R268. doi: 10.1016/j.cub.2024.02.039.

Authors

Tracy Palmer¹, Ben C Berks²

Affiliations

¹ Biosciences Institute, Newcastle University, Newcastle upon Tyne NE2 4HH, UK. Electronic address: Tracy.Palmer@newcastle.ac.uk.
² Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.

PMID: 38593766
DOI: 10.1016/j.cub.2024.02.039

Abstract

In this Quick guide, Palmer and Berks introduce the twin-arginine translocation (Tat) systems. Tats are found in a variety of microbes and microbe-derived organelles, and are known to translocate folded substrate proteins across biological membranes.

MeSH terms

Arginine / metabolism
Bacterial Proteins / metabolism
Cell Membrane / metabolism
Escherichia coli Proteins* / metabolism
Membrane Transport Proteins / genetics
Membrane Transport Proteins / metabolism
Protein Sorting Signals
Protein Transport
Twin-Arginine-Translocation System* / metabolism

Substances

Membrane Transport Proteins
Escherichia coli Proteins
Twin-Arginine-Translocation System
Arginine
Protein Sorting Signals
Bacterial Proteins