UNSPECIFIED (2001) TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli. JOURNAL OF BIOLOGICAL CHEMISTRY, 276 (23). pp. 20213-20219. ISSN 0021-9258

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Abstract

In Escherichia coil, a subset of periplasmic proteins is exported via the twin-arginine translocation (Tat) pathway. In the present study, we have purified the Tat complex from E. coli, and we show that it contains only TatA, TatB, and TatC, Within the purified complex, TatB and TatC are present in a strict 1:1 ratio, suggesting a functional association. This has been confirmed by expression of a translational fusion between TatB and TatC, This Tat(BC) chimera supports efficient Tat-dependent export, indicating that TatB and TatC act as a unit in both structural and functional terms. The purified Tat complex contains varying levels of TatA, suggesting a gradual loss during isolation and a looser association. The molecular mass of the complex is similar to 600 kDa, demonstrating the presence of multiple copies of TatA, B, and C, Co-immunoprecipitation experiments show that TatC is required for the interaction of TatA with TatB, suggesting that TatA may interact with the complex via binding to TatC.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry
Journal or Publication Title:	JOURNAL OF BIOLOGICAL CHEMISTRY
Publisher:	AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
ISSN:	0021-9258
Date:	8 June 2001
Volume:	276
Number:	23
Number of Pages:	7
Page Range:	pp. 20213-20219
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/12093

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