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Assembling the Tat protein translocase

Lookup NU author(s): Professor Tracy Palmer FRS FRSE FMedSciORCiD

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Abstract

© Alcock et al. The twin-arginine protein translocation system (Tat) transports folded proteins across the bacterial cytoplasmic membrane and the thylakoid membranes of plant chloroplasts. The Tat transporter is assembled from multiple copies of the membrane proteins TatA, TatB, and TatC. We combine sequence co-evolution analysis, molecular simulations, and experimentation to define the interactions between the Tat proteins of Escherichia coli at molecular-level resolution. In the TatBC receptor complex the transmembrane helix of each TatB molecule is sandwiched between two TatC molecules, with one of the inter-subunit interfaces incorporating a functionally important cluster of interacting polar residues. Unexpectedly, we find that TatA also associates with TatC at the polar cluster site. Our data provide a structural model for assembly of the active Tat translocase in which substrate binding triggers replacement of TatB by TatA at the polar cluster site. Our work demonstrates the power of co-evolution analysis to predict protein interfaces in multi-subunit complexes.

Publication metadata

Author(s): Alcock F, Stansfeld PJ, Basit H, Habersetzer J, Baker MA, Palmer T, Wallace MI, Berks BC

Publication type: Article

Publication status: Published

Journal: eLife

Year: 2016

Volume: 5

Online publication date: 03/12/2016

Acceptance date: 29/11/2016

Date deposited: 14/02/2019

ISSN (electronic): 2050-084X

Publisher: eLife Sciences Publications Ltd

URL: https://doi.org/10.7554/eLife.20718.001

DOI: 10.7554/eLife.20718.001

PubMed id: 27914200

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