Elsevier

Gene

Volume 151, Issues 1–2, 30 December 1994, Pages 297-301
Gene

Cloning and characterization of the gene encoding the cGMP-phosphodiesterase γ-subunit of human rod photoreceptor cells

https://doi.org/10.1016/0378-1119(94)90674-2Get rights and content

Abstract

Rod photoreceptor cyclic GMP-phosphodiesterase (cGMP-PDE) is one of the key enzymes of the visual phototransduction cascade in the vertebrate retina. The holoenzyme is a heterotetrameric complex, consisting of two large catalytic subunits, a (88 kDa) and β (84 kDa), and two identical inhibitory subunits, γ (11 kDa). Here we present the complete nucleotide sequence of the gene (cGMP-PDEγ) encoding the cGMP-PDE γ-subunit from human rod photoreceptors. The transcribed region of the human cGMP-PDEγ codes for a protein of 87 amino acids and consists of four exons interrupted by three introns. The first intron is located in the 5'-untranslated region. The 5'-flanking region contains TATA-like and CAAT boxes which may serve as regulatory elements. The 5'-untranslated sequence (exon I) includes a potential SP1 transcription factor-binding site (GC core hexanucleotide). In addition, there were five AluI repetitive elements found in the cGMP-PDEγ, three in the first intron and two in the second intron.

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  • Binding of cGMP to GAF domains in amphibian rod photoreceptor cGMP phosphodiesterase (PDE): Identification of GAF domains in PDE αβ subunits and distinct domains in the PDE γ subunit involved in stimulation of cGMP binding to GAF domains

    2002, Journal of Biological Chemistry
    Citation Excerpt :

    However, the ability of Arg24 mutants Pγ(R24E), Pγ(R24H), and Pγ(R24K) to stimulate the level of cGMP binding was similar to that of wild-type Pγ (data not shown), suggesting that Arg24 is not involved in stimulation of cGMP binding. Amino acid 21 in Pγ is not conserved in all known species (28, 58-60). This amino acid appears not to be crucial for Pγ regulation of cGMP binding because bovine and frog Pγ subunits stimulate cGMP binding in a similar way (42), although they have different amino acid residues at position 21 (Fig. 1 C).

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