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Biochim Biophys Acta. 2015 Jan;1848(1 Pt B):260-5. doi: 10.1016/j.bbamem.2014.08.021. Epub 2014 Aug 25.

Cardiolipin interaction with subunit c of ATP synthase: solid-state NMR characterization.

Author information

1
Department of Chemistry, Columbia University, 3000 Broadway, New York, NY 10027, United States.
2
Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Ave., Bronx, NY 10461, United States.
3
Department of Chemistry, Columbia University, 3000 Broadway, New York, NY 10027, United States. Electronic address: aem5@columbia.edu.

Abstract

The interaction of lipids with subunit c from F1F0 ATP synthase is studied by biophysical methods. Subunit c from both Escherichia coli and Streptococcus pneumoniae interacts and copurifies with cardiolipin. Solid state NMR data on oligomeric rings of F0 show that the cardiolipin interacts with the c subunit in membrane bilayers. These studies offer strong support for the hypothesis that F0 has specific interactions with cardiolipin.

KEYWORDS:

ATP synthase; Cardiolipin; Lipid-protein interaction; Solid-state NMR

PMID:
25168468
PMCID:
PMC5526087
DOI:
10.1016/j.bbamem.2014.08.021
[Indexed for MEDLINE]
Free PMC Article

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