O-Crystallin, arginine kinase and ferritin from the octopus lens

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1431, Issue 2, 1999, Pages 512-517

  Zinovieva, Rina D ^a   Piatigorsky, Joram ^a   Tomarev, Stanislav I ^a  

^a NATIONAL EYE INSTITUTE   (United States)

Author keywords

Crystallin; Ferritin; Lens; Octopus; PEBP, phosphatidylethanolamine binding protein; Phosphatidylethanolamine binding protein

Indexed keywords

ARGININE KINASE; BINDING PROTEIN; COMPLEMENTARY DNA; CRYSTALLIN; FERRITIN; LENS PROTEIN; MESSENGER RNA; PHOSPHATIDYLETHANOLAMINE;

AMINO ACID SEQUENCE; ANIMAL TISSUE; ARTICLE; CAENORHABDITIS ELEGANS; CONTROLLED STUDY; DNA LIBRARY; DROSOPHILA; LENS; MOLECULAR WEIGHT; NONHUMAN; NORTHERN BLOTTING; OCTOPUS; ONCHOCERCA VOLVULUS; PRIORITY JOURNAL; VERTEBRATE;

AMINO ACID SEQUENCE; ANIMALS; ARGININE KINASE; CRYSTALLINS; FERRITINS; LENS, CRYSTALLINE; MOLECULAR SEQUENCE DATA; OCTOPODIFORMES; RNA, MESSENGER;

EID: 0032923526     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(99)00066-7     Document Type: Article

References (37)

1. Packard A. Cephalopods and fish: the limits of convergence. Biol. Rev. 47:1972;251-307.
2. Wistow G., Piatigorsky J. Recruitment of enzymes as lens structural proteins. Science. 236:1987;1554-1556.
3. Tomarev S.I., Zinovieva R.D. Squid major lens polypeptides are homologous to glutathione S-transferase subunits. Nature. 336:1988;86-88.
4. Tomarev S.I., Piatigorsky J. Lens crystallins of invertebrates. Diversity and recruitment from detoxification enzymes and novel proteins. Eur. J. Biochem. 235:1996;449-465.
5. Wistow G.J., Piatigorsky J. Lens crystallins: the evolution and expression of proteins for a highly specialized tissue. Annu. Rev. Biochem. 57:1988;479-504.
6. Wistow G. Lens crystallins: gene recruitment and evolutionary dynamism. Trends Biochem. Sci. 18:1993;301-306.
7. Piatigorsky J. Gene sharing in lens and cornea: facts and implications. Prog. Retinal Eye Res. 17:1998;145-174.
8. Siezen R.J., Shaw D.C. Physicochemical characterization of lens proteins of the squid Nototodarus gouldi and comparison with vertebrate crystallins. Biochim. Biophys. Acta. 704:1982;304-320.
9. Tomarev S.I., Chung S., Piatigorsky J. Glutathione S-transferase and S-crystallins of cephalopods: evolution from active enzyme to lens-refractive proteins. J. Mol. Evol. 41:1995;1048-1056.
10. Tomarev S.I., Zinovieva R.D., Piatigorsky J. Crystallins of the octopus lens. Recruitment from detoxification enzymes. J. Biol. Chem. 266:1991;24226-24231.
11. Tomarev S.I., Zinovieva R.D., Piatigorsky J. Characterization of squid crystallin genes. Comparison with mammalian glutathione S-transferase genes. J. Biol. Chem. 267:1992;8604-8612.
12. Zinovieva R.D., Tomarev S.I., Piatigorsky J. Aldehyde dehydrogenase-derived Ω-crystallins of squid and octopus. Specialization for lens expression. J. Biol. Chem. 268:1993;11449-11455.
13. Chiou S.-H. A novel crystallin from octopus lens. FEBS Lett. 241:1988;261-264.
14. Tomarev S.I., Zinovieva R.D., Piatigorsky J. Primary structure and lens-specific expression of genes for an intermediate filament protein and a beta-tubulin in cephalopods. Biochim. Biophys. Acta. 1216:1993;245-254.
15. Schoentgen F., Saccoccio F., Jolles J., Bernier I., Jolles P. Complete amino acid sequence of a basic 21-kDa protein from bovine brain cytosol. Eur. J. Biochem. 166:1987;333-338.
16. Grandy D.K., Hanneman E., Bunzow J., Shih M., Machida C.A., Bidlack J.M., Civelli O. Purification, cloning, and tissue distribution of a 23 kDa rat protein isolated by morphine affinity chromatography. Mol. Endocrinol. 4:1990;1370-1376.
17. Pikielny C.W., Hasan G., Rouyer F., Rosbash M. Members of a family of Drosophila putative odorant-binding proteins are expressed in different subsets of olfactory hairs. Neuron. 12:1994;35-49.
18. Lobos E., Altmann M., Mengod G., Weiss N., Rudin W., Karam M. Identification of an Onchocerca volvulus cDNA encoding a low-molecular-weight antigen uniquely recognized by onchocerciasis patient sera. Mol. Biochem. Parasitol. 39:1990;135-146.
19. Tripp M.L., Bouchard R.A., Pinon R. Cloning and characterization of NSP1, a locus encoding a component of a cdc25-dependent, nutrient-responsive pathway in Saccharomyces cerevisiae. Mol. Microbiol. 3:1989;1319-1327.
20. Cuthbertson R.A., Tomarev S.I., Piatigotsky J. Taxon-specific recruitment of enzymes as major soluble proteins in the corneal epithelium of three mammals, chicken and squid. Proc. Natl. Acad. Sci. USA. 89:1992;4004-4008.
21. Seddiqi N., Bollengier F., Alliel P.M., Perin J.-P., Bonnet F., Bucquoy S., Jolles P., Schoentgen F. Amino acid sequence of the Homo sapiens brain 21-23 kDa protein (neuropolypeptide h3), comparison with its counterparts from Rattus norvegicus and Bos taurus species, and expression of its mRNA in different tissues. J. Mol. Evol. 39:1994;655-660.
22. Wen Y., Li G.W., Chen P., Wong E., Bekhor I. Lens epithelial cell mRNA. II. Expression of a mRNA encoding a lipid-binding protein in rat lens epithelial cells. Gene. 158:1995;269-274.
23. Jaworski C., Wistow G. LP2, a differentiation-associated lipid-binding protein expressed in bovine lens. Biochem. J. 320:1996;49-54.
24. Schoentgen F., Jolles P. From structure to function: possible biological roles of a new widespread protein family binding hydrophobic ligands and displaying a nucleotide binding site. FEBS Lett. 369:1995;22-26.
25. Banfield M.J., Barker J.J., Perry A.C., Brady R.L. Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction. Structure. 6:1998;1245-1254.
26. Serre L., Vallee B., Bureaud N., Schoentgen F., Zelwer C. Crystal structure of the phosphatidylethanolamine-binding protein from bovine brain: a novel structural class of phospholipid-binding proteins. Structure. 6:1998;1255-1265.
27. Dumas C., Camonis J. Cloning and sequence analysis of the cDNA for arginine kinase of lobster muscle. J. Biol. Chem. 268:1993;21599-21605.
28. Suzuki T., Furukohri T. Evolution of phosphagen kinase. Primary structure of glycocyamine kinase and arginine kinase from invertebrates. J. Mol. Biol. 237:1994;353-357.
29. Stein L.D., Harn D.A., David J.R. A cloned ATP:guanidino kinase in the trematode Schistosoma mansoni has a novel duplicated structure. J. Biol. Chem. 265:1990;6582-6588.
30. Friedman D.L., Hejtmancik J.F., Hope J.N., Perryman M.B. Developmental expression of creatine kinase isozymes in mammalian lens. Exp. Eye Res. 49:1989;445-457.
31. Von Darl M., Harrison P.M., Bottke W. cDNA cloning and deduced amino acid sequence of two ferritins: soma ferritin and yolk ferritin, from the snail Lymnaea stagnalis. Eur. J. Biochem. 222:1994;353-366.
32. Dietzel J., Hirzmann J., Preis D., Symmons P., Kunz W. Ferritins of Schistosoma mansoni: sequence comparison and expression in female and male worms. Mol. Biochem. Parasitol. 50:1992;245-254.
33. Lescure A.-M., Proudhoni D., Pesey H., Ragland M., Theil E.C., Briat J.-F. Ferritin gene transcription is regulated by iron in soybean cell cultures. Proc. Natl. Acad. Sci. USA. 88:1991;8222-8826.
34. Boyd D., Vecoli C., Belcher D.M., Jain S.K., Drysdale J.W. Structural and functional relationships of human ferritin H and L chains deduced from cDNA clones. J. Biol. Chem. 260:1985;11755-11761.
35. Harrison P.M., Arosio P. Ferritins: molecular properties, iron storage function and cellular regulation. Biochim. Biophys. Acta. 1275:1996;161-203.
36. Beaumont C., Leneuve P., Devaux I., Scoazec J.Y., Berthier M., Loiseau M.N., Grandchamp B., Bonneau D. Mutation in the iron responsive element of the L ferritin mRNA in a family with dominant hyperferritinaemia and cataract. Nat. Genet. 11:1995;444-446.
37. Didsbury J.R., Theil E.C., Kaufman R.E., Dickey L.F. Multiple red cell ferritin mRNAs, which code for an abundant protein in the embryonic cell type, analyzed by cDNA sequence and by primer extension of the 5′-untranslated regions. J. Biol. Chem. 261:1986;949-955.