Abstract
The TatC protein is an essential component of the bacterial Tat system. By using alkaline phosphatase and β‐glucuronidase fusions we found that TatC contains four transmembrane helices. Three insertions of Ala‐Ser dipeptide at the cytoplasmic N‐ and C‐termini and in the cytoplasmic loop had no or only partial effect on the TatC function. In contrast, five of seven insertions in the two periplasmic loops abolished the Tat function. Four insertions analyzed had no effect on the stability of the altered TatC proteins or on membrane assembly of the TatA and TatB proteins. These data provide a novel base for more detailed studies of the mechanism of the Tat system.
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Dates
Type | When |
---|---|
Created | 22 years, 10 months ago (Oct. 14, 2002, 11:56 a.m.) |
Deposited | 1 year, 11 months ago (Sept. 16, 2023, 1:48 a.m.) |
Indexed | 1 year, 4 months ago (April 7, 2024, 1:17 a.m.) |
Issued | 23 years, 1 month ago (July 16, 2002) |
Published | 23 years, 1 month ago (July 16, 2002) |
Published Online | 23 years, 1 month ago (July 16, 2002) |
Published Print | 23 years ago (Aug. 14, 2002) |
@article{Gouffi_2002, title={Topology determination and functional analysis of the Escherichia coli TatC protein}, volume={525}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/s0014-5793(02)03069-7}, DOI={10.1016/s0014-5793(02)03069-7}, number={1–3}, journal={FEBS Letters}, publisher={Wiley}, author={Gouffi, Kamila and Santini, Claire-Lise and Wu, Long-Fei}, year={2002}, month=jul, pages={65–70} }