Abstract
In bacterial ribosomes, the small (30S) ribosomal subunit is composed of 16S rRNA and 21 distinct proteins. Ribosomal protein S15 is of particular interest because it binds primarily to 16S rRNA and is required for assembly of the small subunit and for intersubunit association, thus representing a key element in the assembly of a whole ribosome. Here we report the 2.8 Å resolution crystal structure of the highly conserved S15–rRNA complex. Protein S15 interacts in the minor groove with a G-U/G-C motif and a three-way junction. The latter is constrained by a conserved base triple and stacking interactions, and locked into place by magnesium ions and protein side chains, mainly through interactions with the unique three-dimensional geometry of the backbone. The present structure gives insights into the dual role of S15 in ribosome assembly and translational regulation.
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Cate, J.H., Yusupov, M.M., Yusupova, G.Zh., Earnest, T.N. & Noller, H. Science 285, 2095–2104 (1999).
Clemons, W.M. Jr. et al. Nature 400, 833– 840 (1999).
Ban, N. et al. Nature 400, 841–847 (1999).
Tocilj, A. et al. Proc. Natl. Acad. Sci. USA 96, 14252– 14257 (1999).
Lee, K., Varma, S. & SantaLucia, J. Jr, Cunningham, P.R. J. Mol. Biol. 269, 732– 743 (1997).
Moazed, D. & Noller, H.F. J. Mol. Biol. 211, 135–145 (1990).
Woodcock, J., Moazed, D., Cannon, M., Davies, J. & Noller, H.F. EMBO J. 10, 3099– 3103 (1991).
Held, W.A., Ballou, B., Micushima, S. & Nomura, M. J. Biol. Chem. 249, 3103–3111 (1974).
Champeney, W.S. Biochim. Biophys. Acta 609, 464–474 (1980).
Culver, G.M., Cate, J.H., Yusupova, G. Zh., Yusupov, M.M. & Noller, H.F. Science 285, 2133–2135 (1999).
Philippe, C. et al. Proc. Natl. Acad. Sci. USA 90, 4396 –4398 (1993).
Serganov, A. et al. RNA 2, 1124–1138 (1996).
Allain, F.H.T. & Varani G., G. J. Mol. Biol. 250, 333–353 ( 1995).
Orr, J.W., Hagerman, P.J. & Williamson, J.R. J. Mol. Biol. 275, 453– 464 (1998).
Powers, T. & Noller, H. RNA 1, 194 –209 (1995).
Batey, R.T. & Willamson, J.R. J. Mol. Biol. 261 , 550–567 (1996).
Clemons, W.M. Jr., Davis, C., White, S.W. & Ramakrishnan, V. Structure 6, 429– 438 (1998).
Berglund, H., Rak, A., Serganov, A., Garber, M. & Hard, T. Nature Struct. Biol. 4, 20– 23 (1997).
Serganov, A. et al. Eur. J. Biochem. 246, 291– 300 (1997).
Bénard, L. et al. Proc. Natl. Acad. Sci. USA 95, 2564 –2567 (1998).
Scott, W.G., Finch, J.T. & Klug, A. Cell 81, 991–1002 (1995).
Batey, R.T. & Willamson, J.R. RNA 4, 984–997 (1998).
Musier-Forsyth, K. et al. Science 253, 784–786 (1991).
Mao, H., White, S. & Williamson, J.R. Nature Struct. Biol. 6, 1139 –1147 (1999).
Conn, G.L., Draper, D.E., Lattman, E.E. & Gittis, A.G. Science 84, 1171–1174 ( 1999).
Wimberly, B.T., Guymon, R., McCutcheon, J.P., White, S.W. & Ramakrishnan, V. Cell 97, 491–502 (1999).
Ehresmann, C. et al. Biochem. Cell. Biol. 73, 1131– 1140 (1995).
Philippe, C. et al. Nucleic Acids Res. 23, 18– 28 (1995).
Otwinowski, Z. & Minor, W. Methods Enzymol. 276A, 307–326 ( 1996).
Collaborative Computational Project, Number 4. Acta Crystallogr. D 50, 760–763 (1994).
de la Fortelle, E. & Bricogne, G. Methods Enzymol. 276A, 472–494 ( 1997).
Abrahams, J.P. & Leslie, A.G.W. Acta Crystallogr. D 42, 905–921 ( 1996).
Jones, T.A., Zhou, J.Y., Cowan, S.W. & Kjeldgaard, M. Acta Crystallogr. A47, 110–119 ( 1991).
Brünger, A.T. et al. Acta Crysallogr. D 54, 905– 921 (1998).
Acknowledgements
We thank E. Westhof, P. Romby and T. Hermann for helpful discussions. We are grateful to the people of beamline BW7A at DESY (Hamburg, Germany). This work was supported by the Russian Academy of Sciences, Russian Foundation for Basic Research, the Centre National de la Recherche Scientifique (CNRS). A.N., A.S. and S.T. were fellows of French–Russian Collaboration Program. A.S. and M.G. were supported in part by the ‘Fondation de la Recherche Médicale’ (FRM) and the International Research Scholar's award from the Howard Hughes Medical Institute, respectively.
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Nikulin, A., Serganov, A., Ennifar, E. et al. Crystal structure of the S15–rRNA complex. Nat Struct Mol Biol 7, 273–277 (2000). https://doi.org/10.1038/74028
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DOI: https://doi.org/10.1038/74028
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