Beta-subunit of bovine rod photoreceptor cGMP phosphodiesterase. Comparison with the phosphodiesterase family

• Published in: The Journal of biological chemistry 1990-08, Vol.265 (22), p.12955-12959
• Main Authors: LIPKIN, V. M, KHRAMTSOV, N. V, VASILEVSKAYA, I. A, ATABEKOVA, N. V, MURADOV, K. G, GUBANOV, V. V, JOHNSTON, J. P, LI, T, VOLPP, K. J, APPLEBURY, M. L
• Format: Article
• Language: English
• Subjects: 3',5'-Cyclic-GMP Phosphodiesterases - genetics; Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; Base Sequence; Biological and medical sciences; Cattle; DNA - genetics; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Gene Library; genes; Hydrolases; Macromolecular Substances; Molecular Sequence Data; Molecular Weight; Multigene Family; Oligonucleotide Probes; Phosphoric Diester Hydrolases - genetics; Photoreceptor Cells - enzymology; Restriction Mapping; Rod Cell Outer Segment - enzymology; Sequence Homology, Nucleic Acid
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(19)38252-3

A group of cDNA clones encoding the beta-subunit of bovine rod photoreceptor cGMP phosphodiesterase were isolated for structural analysis. The encoded polypeptide has 853 residues with a calculated molecular mass of 98 kDa. The beta-subunit is 72% identical to the rod cGMP phosphodiesterase alpha-subunit. Like the alpha-subunit and the cone alpha'-subunit, the beta-subunit belongs to the family of phosphodiesterase genes. The beta- and alpha-subunits are more similar to each other than either is to the cone alpha'-subunit, suggesting either that the beta- and alpha-subunits diverged more recently or that their divergence was restrained by the rod functional environment.