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Science 22 February 1991: Vol. 251. no. 4996, pp. 915 - 918 DOI: 10.1126/science.1672047
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Articles
Science, Vol 251, Issue 4996, 915-918
Copyright © 1991 by American Association for the Advancement of Science
Recoverin: a calcium sensitive activator of retinal rod guanylate cyclase
AM Dizhoor,
S Ray,
S Kumar,
G Niemi,
M Spencer,
D Brolley,
KA Walsh,
PP Philipov,
JB Hurley,
and
L Stryer
Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
Vertebrate retinal photoreceptors recover from photoexcitation-induced hydrolysis of guanosine 3', 5'-monophosphate (cyclic GMP) by resynthesizing cyclic GMP, which reopens cation channels that have been closed by light. Activation of guanylate cyclase by light-induced depletion of cytosolic calcium is a key event in this recovery process. This cyclase has now been shown to be regulated by a 23-kilodalton calcium binding protein. The protein is present in both rod and cone photoreceptors and was named recoverin because it promotes recovery of the dark state. The amino acid sequence of recoverin exhibits three potential calcium binding sites (EF hands). That recoverin binds calcium was confirmed with calcium-45 and by observing calcium-induced changes in its tryptophan fluorescence. Recoverin activated guanylate cyclase when free calcium was lowered from 450 to 40 nM, an effect that was blocked by an antibody to recoverin. Thus, guanylate cyclase in retinal rods is stimulated during recovery by the calcium-free form of recoverin. A comparison of recoverin with other calcium binding proteins reveals that it may represent, along with the protein visinin, a family of proteins that are regulated by submicromolar calcium concentrations.
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