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Transbilayer disposition of the phospholipid annulus surrounding a calcium transport protein

Nature volume 274, pages 823–825 (1978)Cite this article

Abstract

THE lipids that interact with the penetrant surfaces of membrane proteins constitute an important fraction of the lipids in biological membranes: for example, in sarcoplasmic reticulum (SR) vesicles 30 phospholipid molecules are associated with the ATP-dependent calcium transport protein (Ca-ATPase) out of a total of approximately 90 lipids per Ca-ATPase. The lipids in this fraction determine the enzymatic activity of the Ca-ATPase1,2 and they show different physical properties from the remainder of the lipid bilayer2,3; lipids which do not support ATPase activity can be excluded from this fraction4. Similar behaviour has been inferred for the lipids associated with other membrane proteins including rhodopsin5, cytochrome oxidase6 and glycophorin7. These lipids were thought to exist as a single bilayer shell or ‘annulus’ around the protein although no evidence was available to indicate the precise topographical arrangement of the lipids. We describe here a new approach to the identification of this lipid annulus which has allowed us to determine the number of annulus lipids that surround the Ca-ATPase in each monolayer.

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Author notes

  1. J. P. BENNETT

    Present address: Department of Experimental Pathology, University College Hospital Medical School, London, WC1, UK

  2. K. A. McGILL

    Present address: Department of Biochemistry, University of Leeds, 9 Hyde Terrace, Leeds, UK

  3. G. B. WARREN

    Present address: European Molecular Biology Laboratory, Postfach 10.2209, D-6900, Heidelberg, FRG

Authors and Affiliations

  1. Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, UK

    J. P. BENNETT, K. A. McGILL & G. B. WARREN

Authors
  1. J. P. BENNETT
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  2. K. A. McGILL
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  3. G. B. WARREN
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BENNETT, J., McGILL, K. & WARREN, G. Transbilayer disposition of the phospholipid annulus surrounding a calcium transport protein. Nature 274, 823–825 (1978). https://doi.org/10.1038/274823a0

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