PMID: 8953380Dec 1, 1996Paper

Calcium binding to the subunit c of E. coli ATP-synthase and possible functional implications in energy coupling

Journal of Bioenergetics and Biomembranes
S D ZakharovR A Dilley

Abstract

The 8-kDa subunit c of the E. coli F0 ATP-synthase proton channel was tested for Ca++ binding activity using a 45Ca++ ligand blot assay after transferring the protein from SDS-PAGE gels onto polyvinyl difluoride membranes. The purified subunit c binds 45Ca++ strongly with Ca++ binding properties very similar to those of the 8-kDa CF0 subunit III of choloroplast thylakoid membranes. The N-terminal f-Met carbonyl group seems necessary for Ca++ binding capacity, shown by loss of Ca++ binding following removal of the formyl group by mild acid treatment. The dicyclohexylcarbodiimide-reactive Asp-61 is not involved in the Ca++ binding, shown by Ca++ binding being retained in two E. coli mutants, Asp61-->Asn and Asp61-->Gly. The Ca++ binding is pH dependent in both the E. coli and thylakoid 8-kDa proteins, being absent at pH 5.0 and rising to a maximum near pH 9.0. A treatment predicted to increase the Ca++ binding affinity to its F0 binding site (chlorpromazine photoaffinity attachment) caused an inhibition of ATP formation driven by a base-to-acid pH jump in whole cells. Inhibition was not observed when the Ca++ chelator EGTA was present with the cells during the chlorpromazine photoaffinity treatment. An apparent Ca++ binding const...Continue Reading

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Citations

Jan 8, 2013·Current Microbiology·Mohamad KoubarJacques Frère
Feb 6, 2002·Trends in Microbiology·Jan MichielsJos Vanderleyden
Dec 4, 2003·Biochimica Et Biophysica Acta·Ansgar PoetschHolger Seelert
Apr 7, 1999·Molecular Genetics and Metabolism·J E McGeoch, D N Palmer
Feb 13, 2016·Journal of Bioenergetics and Biomembranes·Nelli MnatsakanyanElizabeth A Jonas
May 30, 2009·Journal of Molecular Biology·Pricila HaukChuck Shaker Farah

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