Characterisation and membrane assembly of the TatA component of the Escherichia coli twin-arginine protein transport system

Procelli, Ida, de Leeuw, Erik, Wallis, Russell, van den Brink-van der Laan, Els, de Kruijff, Ben, Wallace, B.A., Palmer, Tracy and Berks, Ben C. (2002) Characterisation and membrane assembly of the TatA component of the Escherichia coli twin-arginine protein transport system. Biochemistry, 41 (46). pp. 13690-13697.

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Abstract

Proteins bearing a signal peptide with a consensus twin-arginine motif are translocated via the Tat pathway, a multiprotein system consisting minimally of the integral inner membrane proteins TatA, TatB, and TatC. On a molar basis, TatA is the major pathway component. Here we show that TatA can be purified independently of the other Tat proteins as a 460 kDa homooligomeric complex. Homooligomer formation requires the amino-terminal membrane-anchoring domain of TatA. According to circular dichroism spectroscopy, approximately half of the TatA polypeptide forms α-helical secondary structure in both detergent solution and proteoliposomes. An expressed construct without the transmembrane segment is largely unstructured in aqueous solution but is able to insert into phospholipid monolayers and interacts with membrane bilayers. Protease accessibility experiments indicate that the extramembranous region of TatA is located at the cytoplasmic face of the cell membrane.

Item Type: Article
Faculty \ School: Faculty of Science > School of Biological Sciences
Depositing User: LivePure Connector
Date Deposited: 08 Jan 2019 11:30
Last Modified: 04 May 2020 23:47
URI: https://ueaeprints.uea.ac.uk/id/eprint/69472
DOI: 10.1021/bi026142i

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