Nucleotide binding to the rod outer segment rim protein.

T A Shuster; A K Nagy; D B Farber

doi:10.1016/s0014-4835(88)80053-8

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Nucleotide binding to the rod outer segment rim protein.

T A Shuster·A K Nagy·D B Farber

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Abstract

The rod photoreceptor outer segment maintains a remarkable morphology. Two of the proteins which have been implicated in the maintenance of this structure are the 240 kDa spectrin-like protein, and the 220 kDa glycoprotein often referred to as the rim protein. We have probed rat rod outer segment proteins with light-activated (azido-labeled) radioactive nucleotides and found a nucleotide binding site(s) on the rim protein which has a preference for guanine nucleotides. Binding to this site is stimulated by the divalent cations zinc, manganese and magnesium, but not calcium. This site is under investigation and may play a role in stabilizing protein structure.

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ATP-Binding Cassette Transporters Adenosine Triphosphate Animals Azides Binding Sites Electrophoresis, Polyacrylamide Gel Eye Proteins Guanosine Triphosphate Magnesium Manganese Membrane Proteins Molecular Weight Photoreceptor Cells Rats Rod Cell Outer Segment Zinc Journal Article Research Support, U.S. Gov't, P.H.S.

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T A Shuster, A K Nagy, D B Farber. 1988. Nucleotide binding to the rod outer segment rim protein.. https://doi.org/10.1016/s0014-4835(88)80053-8

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