Lipid-rhodopsin hydrophobic mismatch alters rhodopsin helical content.

Journal of the American Chemical Society
Olivier SoubiasKlaus Gawrisch

Abstract

The ability of photoactivated rhodopsin to achieve the enzymatically active metarhodopsin II conformation is exquisitely sensitive to bilayer hydrophobic thickness. The sensitivity of rhodopsin to the lipid matrix has been explained by the hydrophobic matching theory, which predicts that lipid bilayers adjust elastically to the hydrophobic length of transmembrane helices. Here, we examined if bilayer thickness adjusts to the length of the protein or if the protein alters its conformation to adapt to the bilayer. Purified bovine rhodopsin was reconstituted into a series of mono-unsaturated phosphatidylcholines with 14-20 carbons per hydrocarbon chain. Changes of hydrocarbon chain length were measured by (2)H NMR, and protein helical content was quantified by synchrotron radiation circular dichroism and conventional circular dichroism. Experiments were conducted on dark-adapted rhodopsin, the photo-intermediates metarhodopsin I/II/III, and opsin. Changes of bilayer thickness upon rhodopsin incorporation and photoactivation were mostly absent. In contrast, the helical content of rhodopsin increased with membrane hydrophobic thickness. Helical content did not change measurably upon photoactivation. The increases of bilayer thicknes...Continue Reading

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Citations

Jun 27, 2012·The Journal of General Physiology·Keith M CallenbergMichael Grabe
Jan 1, 2014·Chemistry and Physics of Lipids·Alexander L BosciaStephanie Tristram-Nagle
Dec 18, 2013·Biochimica Et Biophysica Acta·Daniel Huster
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