Methylation of proteins in photoreceptor rod outer segments.
A set of proteins in bovine rod outer segments is specifically methylated by S-adenosyl-L-methionine. The reaction can be demonstrated in the intact retina as well as in fragmented preparations of isolated rod outer segments. The apparent molecular weights of these proteins are 88,000, 61,000, and a subset between 21,000 and 26,000. The Mr = 88,000 protein is shown to be the alpha subunit of the rod outer segment cGMP phosphodiesterase by peptide mapping, two-dimensional gel electrophoresis, the ionic strength dependence of its interaction with the membrane, and immunoprecipitation by antiserum raised against purified phosphodiesterase. For each of these proteins, the incorporated methyl groups are hydrolyzed in alkali to yield methanol, indicating that the proteins are carboxymethylated.
D015106:3',5'-Cyclic-GMP Phosphodiesterases / Q000378:metabolism; D000818:Animals; D002417:Cattle; D008745:Methylation; D008970:Molecular Weight; D009994:Osmolar Concentration; D010786:Photoreceptor Cells / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*; D012374:Rod Cell Outer Segment / Q000378:metabolism*
D011506:Proteins; D015106:3',5'-Cyclic-GMP Phosphodiesterases