Phosphorylation of ribosomal protein L18 is required for its folding and binding to 5S rRNA

Biochemistry

Volumn 38, Issue 40, 1999, Pages 13385-13390

  Bloemink, Marieke J ^a   Moore, Peter B ^a  

^a YALE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MAGNESIUM ION; RIBOSOME PROTEIN; RNA 5S;

AMINO ACID SEQUENCE; ARTICLE; GEOBACILLUS STEAROTHERMOPHILUS; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN PHOSPHORYLATION; PROTEIN STABILITY;

AMINO ACID SEQUENCE; BACILLUS STEAROTHERMOPHILUS; BACTERIAL PROTEINS; CIRCULAR DICHROISM; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PHOSPHORYLATION; PHOSPHOSERINE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; RIBOSOMAL PROTEINS; RNA, BACTERIAL; RNA, RIBOSOMAL, 5S; TITRIMETRY;

GEOBACILLUS STEAROTHERMOPHILUS;

EID: 0032867611     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9914816     Document Type: Article

References (32)

1. Moore, P. B. (1996) in Ribosomal RNA: Structure, Evolution, Processing and Function in Biosynthesis (Zimmermann, R. A., and Dahlberg, A. E., Eds.) pp 199-236, CRC Press, Boca Raton, FL.
2. Erdmann, V. A., Fahnestock, S., Higo, K., and Nomura, M. (1971) Proc. Natl Acad. Sci. U.S.A. 68, 2932-2936.
3. Christiansen, J., and Garrett, R. A. (1986) in Structure, Function and Genetics of Ribosomes (Hardesty, B., and Krames, G., Eds.) pp 253-269, Springer-Verlag, New York.
4. Dohme, F., and Nierhaus, K. H. (1976) Proc. Natl. Acad. Sci U.S.A. 73, 2221-2225.
5. Spierer, P., Bogdanov, A. A., and Zimmerman, R. A. (1978) Biochemistry 17, 5394-5398.
6. Newberry, V., Brosius, J., and Garrett, R. (1978) Nucleic Acids Res. 5, 1753-1766.
7. Setterquist, R. A., Smith, G. K., Oakley, T. H., Lee, Y., and Fox, G. E. (1996) Gene 183, 237-242.
8. Ramakrishnan, V., and Gerchman, S. E. (1991) J. Biol. Chem. 266, 880-885.
9. Moore, P. B., Abo, S., Freeborn, B., Gewirth, D. T., Leontis, N. B., and Sun, G. (1988) Methods Enzymol. 164, 158-174.
10. Perczel, A., Park, K., and Fasman, G. D. (1992) Anal. Biochem. 203, 83-93.
11. Kay, L. E., Keifer, P., and Saarinen, T. (1992) J. Am. Chem. Soc. 114, 10663-10665.
12. Krishna, R. G., and Wold, F. (1997) in Protein Structure, a Practical Approach (Creighton, T. E., Ed.) p 111, Oxford University Press, Oxford, U.K.
13. Martensen, T. D. (1984) Methods Enzymol. 107, 3-23.
14. Kime, M. J., and Moore, P. B. (1983) Biochemistry 22, 2615-2622.
15. Rost, B., and Sander, C. (1993) J. Mol. Biol. 232, 584-599.
16. Rost, B., Sander, C., and Schneider, R. (1994) CABIOS 10, 53-60.
17. Rost, B., and Sander, C. (1994) Proteins: Struct., Funct., Genet. 19, 55-72.
18. Brauer, M., and Sykes, B. D. (1984) Methods Enzymol. 107, 37-81.
19. Blackburn, B. J., Lapper, R. D., and Smith, I. C. P. (1973) J. Am. Chem. Soc. 95, 2873-2878
20. Ray, W. J., Mildvan, A. S., and Grutzner, J. B. (1977) Arch. Biochem. Biophys. 184, 453.
21. Peyerin, W., Ackermann, K., and Lorenz, P. (1996) in Protein Phosphorylation (Marks, F., Ed.) pp 117-143, VCH Publishers, Inc., New York.
22. Wool, I. G. (1986) in Structure, Function and Genetics of Ribosomes (Hardesty, B., and Kramer, G., Eds.) pp 391-411, Springer-Verlag, New York.
23. Wool, I. G., Chan, Y.-L., and Gluck, A. (1995) Biochem. Cell Biol. 73, 933-947.
24. Kim, J., Cha, J., Marshak, D. R., and Bae, Y. (1996) Biochem. Biophys. Res. Commun. 266, 180-186.
25. Hirano, K., Ito, M., and Hartshorne, D. J. (1995) J. Biol. Chem. 270, 19786-19790.
26. Campos, F., Corona-Reyes, M., and Zinker, S. (1990) Biochim. Biophys. Acta 1087, 142-146.
27. Hershey, J. W. B. (1989) J. Biol. Chem. 264, 20823-20826.
28. Zhang, C. (1996) Mol. Microbiol. 20, 9-15.
29. Cozzone, A. J. (1988) Annu. Rev. Microbiol. 42, 97-125.
30. Guitton, C., Dorne, A., and Mache, R. (1984) Biochem. Biophys. Res. Commun. 121, 297-303.
31. Marks, F. (1996) in Protein Phosphorylation (Marks, F., Ed.) VCH Publishers, Inc., New York.
32. Johnson, L. N., and Barford, D. (1993) Annu. Rev. Biophys. Biomol. Struct. 22, 199-232.