Structure of the TatC core of the twin-arginine protein transport system

Sarah E. Rollauer, Michael J. Tarry, James E. Graham, Mari Jääskeläinen, Franziska Jäger, Steven Johnson, Martin Krehenbrink, Sai Man Liu, Michael J. Lukey, Julien Marcoux, Melanie A. Mcdowell, Fernanda Rodriguez, Pietro Roversi, Phillip J. Stansfeld, Carol Vivien Robinson, Mark S.P. Sansom, Tracy Palmer, Martin Högbom, Ben C. Berks, Susan M. Lea

Research output: Contribution to journalArticleResearchpeer-review

110 Citations (Scopus)

Abstract

The twin-arginine translocation (Tat) pathway is one of two general protein transport systems found in the prokaryotic cytoplasmic membrane and is conserved in the thylakoid membrane of plant chloroplasts. The defining, and highly unusual, property of the Tat pathway is that it transports folded proteins, a task that must be achieved without allowing appreciable ion leakage across the membrane. The integral membrane TatC protein is the central component of the Tat pathway. TatC captures substrate proteins by binding their signal peptides. TatC then recruits TatA family proteins to form the active translocation complex. Here we report the crystal structure of TatC from the hyperthermophilic bacterium Aquifex aeolicus. This structure provides a molecular description of the core of the Tat translocation system and a framework for understanding the unique Tat transport mechanism.

Original languageEnglish
Pages (from-to)210-214
Number of pages5
JournalNature
Volume492
Issue number7428
DOIs
Publication statusPublished - 13 Dec 2012
Externally publishedYes

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