Primary and Secondary Structure of Bovine Retinal S Antigen (48-kDa Protein)

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1987 Oct 1

PMID 3478675

Citations 38

Authors

T Shinohara

B Dietzschold

C M Craft

G Wistow

J J Early

L A Donoso

J Horwitz

R Tao

Affiliations

Soon will be listed here.

Abstract

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 alpha 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 beta-sheet conformation. Acid-catalyzed methanolysis suggests the presence of low levels of carbohydrate in the molecule.

Citing Articles

The Role of Individual Residues in the N-Terminus of Arrestin-1 in Rhodopsin Binding.

Vishnivetskiy S, Paul T, Gurevich E, Gurevich V Int J Mol Sci. 2025; 26(2).

PMID: 39859432 PMC: 11765510. DOI: 10.3390/ijms26020715.

Arrestins: A Small Family of Multi-Functional Proteins.

Gurevich V Int J Mol Sci. 2024; 25(11).

PMID: 38892473 PMC: 11173308. DOI: 10.3390/ijms25116284.

β-arrestin1 promotes tauopathy by transducing GPCR signaling, disrupting microtubules and autophagy.

Woo J, Yan Y, Kee T, Cazzaro S, McGill Percy K, Wang X Life Sci Alliance. 2021; 5(3).

PMID: 34862271 PMC: 8675912. DOI: 10.26508/lsa.202101183.

Mechanistic diversity involved in the desensitization of G protein-coupled receptors.

Sun N, Kim K Arch Pharm Res. 2021; 44(4):342-353.

PMID: 33761113 DOI: 10.1007/s12272-021-01320-y.

GRKs as Modulators of Neurotransmitter Receptors.

Gurevich E, Gurevich V Cells. 2021; 10(1).

PMID: 33396400 PMC: 7823573. DOI: 10.3390/cells10010052.

References

Broekhuyse R, Bessems H . The molecular weight of bovine retinal S-antigen. Exp Eye Res. 1985; 40(5):763-6. DOI: 10.1016/0014-4835(85)90146-0. View

Chang C, Wu C, Yang J . Circular dichroic analysis of protein conformation: inclusion of the beta-turns. Anal Biochem. 1978; 91(1):13-31. DOI: 10.1016/0003-2697(78)90812-6. View

GREENFIELD N, Fasman G . Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry. 1969; 8(10):4108-16. DOI: 10.1021/bi00838a031. View

Nozaki Y, Tanford C . The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale. J Biol Chem. 1971; 246(7):2211-7. View

Chen Y, Yang J, Chau K . Determination of the helix and beta form of proteins in aqueous solution by circular dichroism. Biochemistry. 1974; 13(16):3350-9. DOI: 10.1021/bi00713a027. View

WACKER W, Donoso L, Kalsow C, Yankeelov Jr J, Organisciak D . Experimental allergic uveitis. Isolation, characterization, and localization of a soluble uveitopathogenic antigen from bovine retina. J Immunol. 1977; 119(6):1949-58. View

SANGER F, Nicklen S, Coulson A . DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977; 74(12):5463-7. PMC: 431765. DOI: 10.1073/pnas.74.12.5463. View

Garnier J, Osguthorpe D, Robson B . Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J Mol Biol. 1978; 120(1):97-120. DOI: 10.1016/0022-2836(78)90297-8. View

Kalsow C, WACKER W . Pineal gland involvement in retina-induced experimental allergic uveitis. Invest Ophthalmol Vis Sci. 1978; 17(8):774-83. View

10.

Kuhn H . Light-regulated binding of rhodopsin kinase and other proteins to cattle photoreceptor membranes. Biochemistry. 1978; 17(21):4389-95. DOI: 10.1021/bi00614a006. View

11.

Horwitz J, Bullard B, Mercola D . Interaction of troponin subunits. The interaction between the inhibitory and tropomyosin-binding subunits. J Biol Chem. 1979; 254(2):350-5. View

12.

Higgins R, Dahmus M . Rapid visualization of protein bands in preparative SDS-polyacrylamide gels. Anal Biochem. 1979; 93(2):257-60. DOI: 10.1016/s0003-2697(79)80148-7. View

13.

Nussenblatt R, Gery I, BALLINTINE E, WACKER W . Cellular immune responsiveness of uveitis patients to retinal S-antigen. Am J Ophthalmol. 1980; 89(2):173-9. DOI: 10.1016/0002-9394(80)90108-7. View

14.

Whitaker J, Granum P . An absolute method for protein determination based on difference in absorbance at 235 and 280 nm. Anal Biochem. 1980; 109(1):156-9. DOI: 10.1016/0003-2697(80)90024-x. View

15.

Nussenblatt R, Kuwabara T, de Monasterio F, WACKER W . S-antigen uveitis in primates. A new model for human disease. Arch Ophthalmol. 1981; 99(6):1090-2. DOI: 10.1001/archopht.1981.03930011090021. View

16.

Hewick R, Hunkapiller M, HOOD L, Dreyer W . A gas-liquid solid phase peptide and protein sequenator. J Biol Chem. 1981; 256(15):7990-7. View

17.

Faure J . Autoimmunity and the retina. Curr Top Eye Res. 1980; 2:215-302. View

18.

Mahoney W . Isolation of denatured proteins and peptides by high-performance liquid chromatography. Effect of different perfluorinated acids, column length and large-pore supports. Biochim Biophys Acta. 1982; 704(2):284-9. DOI: 10.1016/0167-4838(82)90158-3. View

19.

Van Dop C, Tsubokawa M, Bourne H, Ramachandran J . Amino acid sequence of retinal transducin at the site ADP-ribosylated by cholera toxin. J Biol Chem. 1984; 259(2):696-8. View

20.

Manning D, Fraser B, Kahn R, GILMAN A . ADP-ribosylation of transducin by islet-activation protein. Identification of asparagine as the site of ADP-ribosylation. J Biol Chem. 1984; 259(2):749-56. View