The Effect of Recombinant Recoverin on the Photoresponse of Truncated Rod Photoreceptors

Recoverin is a heterogeneously acylated calcium-binding protein thought to regulate visual transduction. Its effect on the photoresponse was investigated by dialyzing the recombinant protein into truncated salamander rod outer segments. At high Ca2+(Ca), myristoylated recoverin (Ca-recoverin) prolon...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1998-05, Vol.95 (11), p.6474-6479
Main Authors: Erickson, Martha A., Lagnado, Leon, Zozulya, Sergey, Neubert, Thomas A., Stryer, Lubert, Baylor, Denis A.
Format: Article
Language:English
Subjects:
Ambystoma
Animals
Biological Sciences
Calcium
Calcium - physiology
Calcium-Binding Proteins - pharmacology
Coefficients
Electrodes
Eye Proteins
Eyes & eyesight
Fatty acids
Hippocalcin
Least squares
Light
Lipoproteins
Nerve Tissue Proteins
Neurobiology
Neurology
Neuroscience
Phosphorylation
Proteins
Recombinant Proteins - pharmacology
Recoverin
Retinal Rod Photoreceptor Cells - drug effects
Retinal Rod Photoreceptor Cells - physiology
Salamanders
Time constants
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Summary:Recoverin is a heterogeneously acylated calcium-binding protein thought to regulate visual transduction. Its effect on the photoresponse was investigated by dialyzing the recombinant protein into truncated salamander rod outer segments. At high Ca2+(Ca), myristoylated recoverin (Ca-recoverin) prolonged the recovery phase of the bright flash response but had less effect on the dim flash response. The prolongation of recovery had an apparent Kdfor Ca of 13 μ M and a Hill coefficient of 2. The prolongation was shown to be mediated by inhibition of rhodopsin deactivation. After a sudden imposed drop in Ca concentration, the effect of recoverin switched off with little lag. The myristoyl (C14:0) modification of recoverin increased its activity 12-fold, and the C12:0 or C14:2 acyl group gave similar effects. These experiments support the notion that recoverin mediates Ca-dependent inhibition of rhodopsin phosphorylation and thereby controls light-triggered phosphodiesterase activity, particularly at high light levels.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.95.11.6474