PMID: 2497769Feb 21, 1989Paper

Rhodopsin-G-protein interactions monitored by resonance energy transfer

Biochemistry
H Borochov-Neori, M Montal

Abstract

Resonance energy transfer measurements were implemented to monitor the specific interactions between G-protein and rhodopsin in phospholipid vesicles reconstituted with the purified proteins. Fluorescently labeled G-protein was extracted from bleached rod outer segments (ROS) reacted with several sulfhydryl reagents: N-(1-pyrenyl)maleimide (P), monobromobimane (B), 7-(diethylamino)-3-(4-maleimidylphenyl)-4-methylcoumarin (C), and N-(4-anilino-1-naphthyl)maleimide (A). Limited labeling of ROS, resulting in the modification of less than a single -SH residue per G-protein molecule and less than 0.2 residue per rhodopsin, did not impair the specific in situ interactions between rhodopsin and G-protein. This was demonstrated by preservation of their light-activated tight association and Gpp(NH)p binding and their fast dissociation with excess GTP. The distribution of fluorescent label among the three subunits of G-protein revealed a highly reactive -SH group in the gamma subunit accessible to labeling when G-protein was bound specifically to bleached rhodopsin. Recombination of purified fluorescent derivatives of G-protein with purified rhodopsin reconstituted in lipid vesicles restored the light-activated Gpp(NH)p binding to a leve...Continue Reading

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Citations

Mar 15, 1992·European Journal of Biochemistry·H HeithierE J Helmreich
Nov 5, 2013·Biochimica Et Biophysica Acta·Ulrike Alexiev, David L Farrens
Jan 31, 1998·Analytical Biochemistry·A L ParolaB K Kobilka
Oct 3, 2006·Biophysical Journal·Ana Vitória BotelhoMichael F Brown
May 1, 1994·Protein Science : a Publication of the Protein Society·S J HubbardJ M Thornton
Nov 17, 2020·Macromolecular Rapid Communications·Hanna TraegerStephen Schrettl

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