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Membrane topology of the MotA protein of Escherichia coli.

Abstract：

:The MotA protein of Escherichia coli is a component of the flagella that functions together with the MotB protein in transmembrane proton conduction. It is an integral membrane protein, with four hydrophobic segments that might traverse the membrane and two short segments that are predicted to be in the periplasm. In a previous study of the accessibility of MotA to various proteases, evidence for periplasmic segments was not obtained, probably because they are small. Here, we report site-directed sulfhydryl labeling experiments which show that two segments of MotA are exposed on the periplasmic side of the membrane, while the rest of the protein is in the cytoplasm. These experiments establish that the main features of the suggested model for MotA topology are correct, furnishing a basis for more detailed structure-function studies of the MotA/MotB proton channel.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Zhou J,Fazzio RT,Blair DF

doi

10.1006/jmbi.1995.0431

subject

Has Abstract

pub_date

1995-08-11 00:00:00

pages

237-42

issue

2

eissn

0022-2836

issn

1089-8638

pii

S0022283685704317

journal_volume

251

pub_type

杂志文章

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