Isolation and expression of the genes encoding the acidic ribosomal phosphoproteins P1 and P2 of the medfly Ceratitis capitata

Gene

Volumn 226, Issue 2, 1999, Pages 365-373

  Gagou, Mary Elisabeth ^a   Rodriguez Gabriel, M A ^b   Ballesta, Juan P G ^b   Kouyanou, Sophia ^a  

^a UNIVERSITY OF ATHENS   (Greece)

^b CSIC   (Spain)

Author keywords

E. coli; Heterologous expression; Molecular cloning; Phosphorylation; Ribosomal proteins; Sequence comparison

Indexed keywords

RIBOSOME PROTEIN; RIBOSOME PROTEIN P1; RIBOSOME PROTEIN P2; UNCLASSIFIED DRUG;

ARTICLE; ESCHERICHIA COLI; EUKARYOTE; GENE EXPRESSION; MEDITERRANEAN FRUIT FLY; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN ISOLATION; RIBOSOME; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; BINDING SITES; CLONING, MOLECULAR; DIPTERA; DNA, COMPLEMENTARY; ESCHERICHIA COLI; GUANOSINE TRIPHOSPHATE; MOLECULAR SEQUENCE DATA; PHOSPHOPROTEINS; RIBOSOMAL PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

CAPITATA; CERATITIS CAPITATA; DROSOPHILA MELANOGASTER; ESCHERICHIA COLI; EUKARYOTA; HEXAPODA; INSECTA; MELANOGASTER;

EID: 0033590618     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(98)00546-0     Document Type: Article

References (29)

1. Amaldi, F., Pierandrei-Amaldi, P., 1997. TOP genes: A translationally controlled class of genes including those coding for ribosomal proteins. In: Jeanteur, Ph. (Ed.), Progress in Molecular and Subcellular Biology, vol. 18. Springer, Berlin, pp. 1-17.
2. Bailey-Serres J., Vangala S., Szick K., Lee C.H. Acidic phosphoprotein complex of the 60S ribosomal subunit of Maize seedling roots. Plant Physiol. 114:1997;1293-1305.
3. Ballesta J.P.G., Remacha M. The large ribosomal subunit stalk as a regulatory element of the eucaryotic translational machinery. Progr. Nucleic Acids Res. Mol. Biol. 55:1996;157-193.
4. Beltrame M., Bianchi M.E. A gene family for acidic ribosomal proteins in Schizosaccharomyces pombe: Two essential and two non essential genes. Mol. Cell. Biol. 10:1990;2341-2348.
5. Bocharov E.V., Gudkov A.T., Arseniev A.S. Topology of the secondary structure elements of ribosomal protein L7/L12 from E. coli in solution. FEBS Lett. 379:1996;291-294.
6. Hasler P., Brot N., Weisbach H., Parnassa A.P., Elkon K.B. Ribosomal proteins P0, P1, and P2 are phosphorylated by casein kinase II at their conserved carboxyl termini. J. Biol. Chem. 266:1991;13815-13820.
7. Kay M.A., Jacobs-Lorena M. Selective translational regulation of ribosomal protein gene expression during early development of Drosophila melanogaster. Mol. Cell. Biol. 5:1985;3583-3592.
8. Kouyanou S., Gagou M.E., Fragoulis E.G. Characterization of acidic ribosomal proteins from three developmental stages of the medfly Ceratitis capitata. Biochem. Mol. Biol. Int. 45:1998;623-633.
9. Kudlicki W., Szyszka R., Palen E., Gasior E. Evidence for a highly specific protein kinase phosphorylating two strongly acidic proteins of yeast 60S ribosomal subunit. Biochim. Biophys. Acta. 633:1980;376-385.
10. Lavergne J.P., Reboud A.M., Sontag B., Guillot D., Reboud J.P. Binding of GDP to a ribosomal protein after elongation factor-2 dependent GTP hydrolysis. Biochim. Biophys. Acta. 1132:1992;284-289.
11. Liljas A. Comparative biochemistry and biophysics of ribosomal proteins. Int. Rev. Cytol. 124:1991;103-136.
12. Meyuhas, O., Avni, D., Shama, S., 1996. Translational control of ribosomal protein mRNAs in eucaryotes. In: Hershey, J.W.B., Mathews, M., Sonenberg, N. (Eds.), Translational Control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 363-388.
13. Olson P.F., Salo T., Garrison K., Fessler J.H. Drosophila acidic ribosomal protein rpA2: sequence and characterization. J. Cell. Biochem. 51:1993;353-359.
14. Pilecki M., Grankowski N., Jacobs J., Gasior E. Specific protein kinase from Saccharomyces cerevisiae cells phosphorylating 60S ribosomal proteins. Eur. J. Biochem. 206:1992;259-267.
15. Pustell J., Kafatos F.C. A convenient and adaptable package of computer programs for DNA and protein sequence management, analysis and homology determination. Nucleic Acids Res. 12:1984;643-655.
16. Qian S., Zhang J.Y., Kay M.A., Jacobs-Lorena M. Structural analysis of the Drosophila rpA1 gene, a member of the eucaryotic 'A' type ribosomal protein family. Nucleic Acids Res. 15:1987;987-1003.
17. Qian S., Hongo S., Jacobs-Lorena M. Antisense ribosomal protein gene expression specifically disrupts oogenesis in Drosophila melanogaster. Proc. Natl. Acad. Sci. USA. 85:1988;9601-9605.
18. Remacha M., Saenz-Robles M.T., Vilella M.D., Ballesta J.P.G. Independent genes coding for three acidic proteins of the large ribosomal subunit from Saccharomyces cerevisiae. J. Biol. Chem. 263:1988;9094-9101.
19. Rina M., Savakis C. A cluster of vitellogenin genes in the mediterranean fruit fly Ceratitis capitata: sequence and structural conservation in diptera yolk proteins and their genes. Genetics. 127:1991;769-780.
20. Saenz-Robles M.T., Remacha M., Vilella M.D., Zinker S., Ballesta J.P.G. The acidic ribosomal proteins as regulators of the eucaryotic ribosomal activity. Biochim. Biophys. Acta. 1050:1990;51-55.
21. Santos C., Ortiz-Reyes B.L., Naranda T., Remacha M., Ballesta J.P.G. The acidic phosphoproteins from Saccharomyces cerevisiae ribosomes. NH2-terminal acetylation is a conserved difference between P1 and P2 proteins. Biochemistry. 32:1993;4231-4236.
22. Stark H., Rodnina M.V., Rinke A.J., Brimacombe R., Wintermeyer W., van Heel M. Nature. 389:1997;403-406.
23. Szyszka R., Bou G., Ballesta J.P.G. RAP kinase, a new enzyme phosphorylating the acidic P proteins from Saccharomyces cerevisiae. Biochim. Biophys. Acta. 1293:1996;213-221.
24. Tsurugi K., Ogata K. Evidence for the exchangeability of acidic ribosomal proteins on cytoplasmic ribosomes in regenerating rat liver. J. Biochem. 98:1985;1427-1431.
25. Vilella M.D., Remacha M., Ortiz B.L., Mendez E., Ballesta J.P.G. Characterization of the yeast acidic ribosomal phosphoproteins using monoclonal antibodies. Proteins L44/L45 and L44′ have different functional roles. Eur. J. Biochem. 196:1991;407-414.
26. Wool I.G., Chan Y.L., Gluck A., Suzuki K. The primary structure of rat ribosomal proteins P0, P1 and P2 and a proposal for a uniform nomenclature for mammalian and yeast ribosomal proteins. Biochimie. 73:1991;861-870.
27. Zambrano R., Briones E., Remacha M., Ballesta J.P.G. Phosphorylation of the acidic ribosomal P proteins in Saccharomyces cerevisiae: A reappraisal. Biochemistry. 36:1997;14439-14446.
28. Zinker S., Warner J.R. The ribosomal proteins of Saccharomyces cerevisiae phosphorylated and exchangeable proteins. J. Biol. Chem. 251:1976;1799-1807.
29. Zurdo J., Sanz J.M., Gonzalez C., Rico M., Ballesta J.P.G. The exchangeable yeast ribosomal acidic protein YP2β shows characteristics of a partly folded state under physiological conditions. Biochemistry. 36:1997;9625-9635.