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Photoreceptor rod outer segment 48-kDa protein has ATPase activity

Published online by Cambridge University Press:  02 June 2009

Ari Sitaramayya  and
Shereen Hakki
Ari Sitaramayya
Affiliation:
Department of Basic Sciences, Pennsylvania College of Optometry, Philadelphia
Shereen Hakki
Affiliation:
Department of Basic Sciences, Pennsylvania College of Optometry, Philadelphia
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Abstract

The role of 48-kDa protein in Visual transduction remains unresolved. Two hypotheses for its role in quenching the light activation of cyclic GMP cascade suggest that the protein binds to either phosphodiesterase or phosphorylated rhodopsin. Since the protein is also reported to bind ATP, we anticipated that the protein may have ATP hydrolyzing activity, and in analogy with the GTP-binding protein of the rod outer segments, such activity may be greatly enhanced by the elements of transduction cyclic GMP cascade, permitting the protein to function cyclically as GTP-binding protein does. We found that purified 48-kDa protein hydrolyzes ATP but at a slow rate of 0.04–0.05 per min. The Km for ATP is about 45–65 μM. The activity is inhibited noncompetitively by ADP with a Ki of about 50 μM. The ATPase activity of 48-kDa protein is not affected by rhodopsin, bleached rhodopsin, phosphorylated rhodopsin, unactivated cyclic GMP phosphodiesterase, or phosphodiesterase (PDE) activated by GMP PNP-bound G-protein. These data show that although 48-kDa protein has ATPase activity, lack of regulation of this activity by the elements of visual transduction makes it unlikely for this activity to have a role in quenching the light activation of cyclic GMP cascade.

Keywords

PhotoreceptorArrestinRhodopsinG-proteinPhosphodiesterase
Type
Research Article
Information
Visual Neuroscience , Volume 5 , Issue 6 , December 1990 , pp. 585 - 589
Copyright
Copyright © Cambridge University Press 1990

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