Biochemistry (Moscow)

, Volume 69, Issue 12, pp 1319–1323 | Cite as

Role of N-terminal helix in interaction of ribosomal protein S15 with 16S rRNA

Article

Abstract

The position and conformation of the N-terminal helix of free ribosomal protein S15 was earlier found to be modified under various conditions. This variability was supposed to provide the recognition by the protein of its specific site on 16S rRNA. To test this hypothesis, we substituted some amino acid residues in this helix and assessed effects of these substitutions on the affinity of the protein for 16S rRNA. The crystal structure of the complex of one of these mutants (Thr3Cys S15) with the 16S rRNA fragment was determined, and a computer model of the complex containing another mutant (Gln8Met S15) was designed. The available and new information was analyzed in detail, and the N-terminal helix was concluded to play no significant role in the specific binding of the S15 protein to its target on 16S rRNA.

Key words

RNA-protein interactions ribosomal proteins crystal structure S15 protein 16S ribosomal RNA 

REFERENCES

  1. 1.
    Ban, N., Nissen, P., Hansen, J., Moore, P. B., Steitz, T. A. 2000Science289905920Google Scholar
  2. 2.
    Wimberly, B. T., Brodersen, D. E., Clemons, W.M.,Jr., Morgan-Warren, R., Carter, A. P., Vonrhein, C., Hartsch, T., Ramakrishnan, V. 2000Nature407327339Google Scholar
  3. 3.
    Serganov, A., Rak, A., Garber, M., Reinbolt, J., Ehresmann, B., Ehresmann, C., Grunberg-Manago, M., Portier, C. 1997Eur. J. Biochem.246291300Google Scholar
  4. 4.
    Nikulin, A., Serganov, A., Ennifar, E., Tishchenko, S., Nevskaya, N., Shepard, W., Portier, C., Garber, M., Ehresmann, B., Ehresmann, C., Nikonov, N., Dumas, P. 2000Nature Struct. Biol.7273277Google Scholar
  5. 5.
    Garber, M., Gongadze, G., Meshcheryakov, V., Nikonov, O., Nikulin, A., Perederina, A., Piendl, W., Serganov, A., Tishchenko, S. 2002Acta Crystallogr. D Biol. Crystallogr.5816641669Google Scholar
  6. 6.
    Ducruix, A., and Giege, R. (1997) Crystallization of Nucleic Acids and Proteins. A Practical Approach, Oxford University Press.Google Scholar
  7. 7.
    Otwinowski, Z., and Minor, W. (1997) Meth. Enzymol., Vol. 276, Macromolecular Crystallography (Carter, C. W., Jr., and Sweet, R. M., eds.) Pt. A, Academic Press, pp.307–326.Google Scholar
  8. 8.
    Brunger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J.-S., Kuszewski, J., Nilges, N., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T., Warren, G. L. 1998Acta Crystallogr.D54905921Google Scholar
  9. 9.
    Berglund, H., Rak, A., Serganov, A., Garber, M., Hard, T. 1997Nature Struct. Biol.42023Google Scholar
  10. 10.
    Clemons, W.M.,Jr., Davies, C., White, S. W., Ramakrishnan, V. 1998Structure6429438Google Scholar
  11. 11.
    Agalarov, S. V., Prasad, G. S., Funke, P. V., Stout, C. D., Williamson, J. R. 2000Science288107112Google Scholar
  12. 12.
    Serganov, A., Ennifar, E., Portier, C., Ehresmann, B., Ehresmann, C. 2002J. Mol. Biol.320963978Google Scholar

Copyright information

© MAIK “Nauka/Interperiodica” 2004

Authors and Affiliations

  • S. V. Revtovich
    • 1
  • A. D. Nikulin
    • 1
  • S. V. Nikonov
    • 1
  1. 1.Institute of Protein ResearchRussian Academy of SciencesPushchino, Moscow RegionRussia

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