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The beta subunit of the Escherichia coli ATP synthase exhibits a tight membrane binding property.

作者信息

Aris J P, Simoni R D

出版信息

Biochem Biophys Res Commun. 1985 Apr 16;128(1):155-62. doi: 10.1016/0006-291x(85)91658-4.

DOI:10.1016/0006-291x(85)91658-4
PMID:2859019
Abstract

We have developed a chromatographic procedure to analyze the association of the subunits of the Escherichia coli F1Fo-ATP synthase with the cytoplasmic membrane. Minicells containing [35S]-labeled ATP synthase subunits are treated with lysozyme, solubilized, and chromatographed on a Sepharose CL-2B column in buffer containing urea and taurodeoxycholate. ATP synthase subunits are resolved into membrane intrinsic and membrane extrinsic subunits. Interestingly, a significant amount (36%) of the F1 subunit beta fractionates with the membrane intrinsic Fo subunits. About half of this amount (19%) of beta is non-specifically bound to the membrane. Interaction of beta with the membrane is not mediated by the amino terminal portion of beta.

摘要

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