Sequence analysis of bovine retinal S‐antigen

Wistow, Graeme; Katial, Albine; Craft, Cheryl M.; Shinohara, Toshimichi

doi:10.1016/0014-5793(86)80207-1

Cited by 88 publications

(13 citation statements)

References 27 publications

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“…Indeed, the existence of an activity involved in deactivating ligand-activated receptors after removal of the stimulus had long been postulated (39). Interestingly, the predicted amino acid sequence of both human and bovine arrestins revealed regions of amino acid sequence homology with the a subunit of transducin, suggesting that these proteins may compete for a common binding site on rhodopsin (17,(40)(41)(42) arrestin (4). It is interesting to note that vertebrate and invertebrate arrestins are far more conserved when compared with each other (42% amino acid identity; see Fig.…”

Section: Resultsmentioning

confidence: 99%

Isolation and structure of an arrestin gene from Drosophila.

Smith

Shieh

Zuker

1990

Proc. Natl. Acad. Sci. U.S.A.

113

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A Drosophila gene encoding a homologue of vertebrate arrestin was isolated by subtractive hybridization and identified as a member of a set of genes that are preferentially expressed in the visual system. This gene encodes a 364-amino acid protein that displays >40% amino acid sequence identity with human and bovine arrestin. Interestingly, the Drosophila homologue lacks the C-terminal sequences that were postulated to interact with rhodopsin during the quenching of the phototransduction cascade in the vertebrate visual response. These findings are discussed in terms of invertebrate phototransduction. The Drosophila gene was mapped cytogenetically to chromosomal position 36D1-2, near the ninaD locus. However, the arrestin gene does not appear to be the ninaD locus, as sequence analysis of three ethylmethane sulfateinduced ninaD mutant alleles reveals no alteration in amino acid sequence.Phototransduction is the process that converts the energy of an absorbed photon into a change of the ionic permeabilities of the photoreceptor cell membrane. This light-induced change in ionic conductances gives rise to the receptor potential and synaptic activity of the photoreceptor cell. The mechanism of visual excitation in vertebrate photoreceptors is the best understood of all sensory transduction processes (1-4). Light activation of rhodopsin is the first step in the visual response. In the vertebrate, photoactivated rhodopsin molecules activate a guanine nucleotide-binding (G) protein, transducin, which in turn activates a cGMP phosphodiesterase. The reduction of intracellular levels of cGMP leads to the transient closure of a cGMP-gated cation-selective channel and hyperpolarization of the photoreceptor cell.Unlike vertebrates, the microvillar photoreceptors of invertebrates depolarize in response to light and thus open their cation-selective channels. The identity of the intracellular transmitter(s) that mediates excitation in invertebrates has eluded firm identification. Similarly, the enzyme cascade that triggers the visual response has not been defined. However, there is a large body of physiological, genetic, and biochemical work that has strongly implicated calcium and inositol phospholipid metabolism in excitation of dipteran and Limulus photoreceptors (5-7). It is believed that photoactivated rhodopsin interacts with a G protein, which in turn activates a phospholipase C. Phospholipase C would then catalyze the generation of the second messenger inositol 1,4,5-trisphosphate and the subsequent mobilization of calcium from intracellular storage sites. The transient increase in calcium levels (or inositol 1,4,5-trisphosphate) would then lead to the opening of a cation-selective channel and the generation of a depolarizing receptor potential. Strong support for this model was recently provided by the demonstration that the Drosophila no-receptor potential A (norpA) gene encodes a phospholipase C that is abundantly expressed in the adult retina (8,9

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Section: Resultsmentioning

confidence: 99%

Isolation and structure of an arrestin gene from Drosophila.

Smith

Shieh

Zuker

1990

Proc. Natl. Acad. Sci. U.S.A.

113

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“…An additional Xgtl0 library was provided by J. Nathans (Stanford, CA). The methods for isolation of cDNA clones from these libraries have been described (23,24).…”

Section: Methodsmentioning

confidence: 99%

Primary and secondary structure of bovine retinal S antigen (48-kDa protein).

Shinohara

Dietzschold

Craft

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

181

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The complete amino acid sequence of bovine S antigen (48-kDa protein) has been determined by cDNA and partial amino acid sequencing. A 1623-base-pair (bp) cDNA contains an open reading frame coding for a protein of 404 amino acids (45,275 Da). Tryptic peptides and cyanogen bromide peptides of native bovine S antigen were purified and partially sequenced. All of these peptides were accounted for in the long open reading frame. Searching of the National Biomedical Research Foundation data bank revealed no extensive sequence homology between S antigen and other proteins. However, there are local regions of sequence similarity with a transducin, including the sites subject to ADP-ribosylation by Bordetella pertussis and cholera toxins and the phosphoryl binding-sites. Secondary structure prediction and circular dichroic spectroscopy show that S antigen is composed predominantly of a-sheet conformation. Acid-catalyzed methanolysis suggests the presence of low levels of carbohydrate in the molecule.

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“…The carboxyl-terminal region of G-a was postulated to be involved in receptor coupling by Masters et al [4] based on several lines of evidence. Homology of the tr-subunit of the retinal Gprotein, transducin, with arrestin, the '48 kDa' protein of retina which competes with transducin for binding to photo-rhodopsin, is confined to the carboxyl-terminal region of c~-transducin [4,5]. Furthermore G-ct subunits which are functionall3/ uncoupled from receptors by pertussis toxin undergo a mono-ADP-ribosylation at a cysteine residue four amino acids from the carboxylterminus [1][2][3].…”

Section: Introductionmentioning

confidence: 99%

Receptor and effector interactions of G_s Functional studies with antibodies to the α_s carboxyl‐terminal decapeptide

et al. 1989

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Antibodies generated to a synthetic decapeptide, RMHLRQYELL, representing the carboxyl-terminus of Gs-ct have been characterized in immunoblots and functional studies. This antibody, designated RM, reacts exclusively with a doublet of proteins of 52 and 45 kDa in immunoblots of bovine brain and wild-type $49 murine lymphoma cell membranes. No such reactivity is seen in membranes from cyc-$49 cells, which lack Gs. RM blocks receptor-mediated activation of Gs and adenylyl cyclase in membranes from wild-type $49 cells. RM could also immunoprecipitate adenylyl cyclase activity in detergent extracts from GTP[),]S-or fluoride-preactivated bovine brain membranes; thus binding of cts to effector and carboxyl-terminal antibody was mutually compatible. Such experiments provide an approach for the elucidation of functionally relevant interactions of G-proteins with receptors and effectors in the membrane.

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Sequence analysis of bovine retinal S‐antigen

Cited by 88 publications

References 27 publications

Isolation and structure of an arrestin gene from Drosophila.

Isolation and structure of an arrestin gene from Drosophila.

Primary and secondary structure of bovine retinal S antigen (48-kDa protein).

Receptor and effector interactions of G_s Functional studies with antibodies to the α_s carboxyl‐terminal decapeptide

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Sequence analysis of bovine retinal S‐antigen

Cited by 88 publications

References 27 publications

Isolation and structure of an arrestin gene from Drosophila.

Isolation and structure of an arrestin gene from Drosophila.

Primary and secondary structure of bovine retinal S antigen (48-kDa protein).

Receptor and effector interactions of Gs Functional studies with antibodies to the αs carboxyl‐terminal decapeptide

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Product

Resources

About

Receptor and effector interactions of G_s Functional studies with antibodies to the α_s carboxyl‐terminal decapeptide