Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
American Association for Cancer Research

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 7 April 2000:
Vol. 288. no. 5463, pp. 107 - 112
DOI: 10.1126/science.288.5463.107
Prev | Table of Contents | Next

Research Articles

Structure of the S15,S6,S18-rRNA Complex: Assembly of the 30S Ribosome Central Domain

Sultan C. Agalarov, 12* G. Sridhar Prasad, 3* Peter M. Funke, 14* C. David Stout, 3dagger James R. Williamson 1dagger

The crystal structure of a 70-kilodalton ribonucleoprotein complex from the central domain of the Thermus thermophilus 30S ribosomal subunit was solved at 2.6 angstrom resolution. The complex consists of a 104-nucleotide RNA fragment composed of two three-helix junctions that lie at the end of a central helix, and the ribosomal proteins S15, S6, and S18. S15 binds the ribosomal RNA early in the assembly of the 30S ribosomal subunit, stabilizing a conformational reorganization of the two three-helix junctions that creates the RNA fold necessary for subsequent binding of S6 and S18. The structure of the complex demonstrates the central role of S15-induced reorganization of central domain RNA for the subsequent steps of ribosome assembly.

1 Department of Molecular Biology and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
2 Institute for Protein Research, Pushchino, Russia.
3 Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
4 Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
*   These authors contributed equally to this work.

dagger    To whom correspondence should be addressed. E-mail: dave{at}scripps.edu, jrwill{at}scripps.edu

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Anti-Peptide Antibodies for Examining the Conformation, Molecular Assembly and Localization of an Intracellular Protein, Ribosomal Protein S6, In vivo.
M. Nakagawa, N. Ohmido, K. Ishikawa, S. Uchiyama, K. Fukui, and T. Azuma (2008)
J. Biochem. 143, 325-332
   Abstract »    Full Text »    PDF »
Binding of the Human Prp31 Nop Domain to a Composite RNA-Protein Platform in U4 snRNP.
S. Liu, P. Li, O. Dybkov, S. Nottrott, K. Hartmuth, R. Luhrmann, T. Carlomagno, and M. C. Wahl (2007)
Science 316, 115-120
   Abstract »    Full Text »    PDF »
30S ribosomal subunits can be assembled in vivo without primary binding ribosomal protein S15.
M. Bubunenko, A. Korepanov, D. L. Court, I. Jagannathan, D. Dickinson, B. R. Chaudhuri, M. B. Garber, and G. M. Culver (2006)
RNA 12, 1229-1239
   Abstract »    Full Text »    PDF »
Topology of three-way junctions in folded RNAs..
A. LESCOUTE and E. WESTHOF (2006)
RNA 12, 83-93
   Abstract »    Full Text »    PDF »
Protein content of minimal and ancestral ribosome.
A. MUSHEGIAN (2005)
RNA 11, 1400-1406
   Abstract »    Full Text »    PDF »
Molecular Dynamics of a Protein Surface: Ion-Residues Interactions.
R. Friedman, E. Nachliel, and M. Gutman (2005)
Biophys. J. 89, 768-781
   Abstract »    Full Text »    PDF »
The N-terminal extension of Escherichia coli ribosomal protein L20 is important for ribosome assembly, but dispensable for translational feedback control.
M. GUILLIER, F. ALLEMAND, M. GRAFFE, S. RAIBAUD, F. DARDEL, M. SPRINGER, and C. CHIARUTTINI (2005)
RNA 11, 728-738
   Abstract »    Full Text »    PDF »
Nonbridging phosphate oxygens in 16S rRNA important for 30S subunit assembly and association with the 50S ribosomal subunit.
S. GHOSH and S. JOSEPH (2005)
RNA 11, 657-667
   Abstract »    Full Text »    PDF »
Long-Residency Hydration, Cation Binding, and Dynamics of Loop E/Helix IV rRNA-L25 Protein Complex.
K. Reblova, N. Spackova, J. Koca, N. B. Leontis, and J. Sponer (2004)
Biophys. J. 87, 3397-3412
   Abstract »    Full Text »    PDF »
Simulation, experiment, and evolution: Understanding nucleation in protein S6 folding.
I. A. Hubner, M. Oliveberg, and E. I. Shakhnovich (2004)
PNAS 101, 8354-8359
   Abstract »    Full Text »    PDF »
A three-fluorophore FRET assay for high-throughput screening of small-molecule inhibitors of ribosome assembly.
D. Klostermeier, P. Sears, C.-H. Wong, D. P. Millar, and J. R. Williamson (2004)
Nucleic Acids Res. 32, 2707-2715
   Abstract »    Full Text »    PDF »
How Bacterial Ribosomal Protein L20 Assembles with 23 S Ribosomal RNA and Its Own Messenger RNA.
S. Raibaud, P. Vachette, M. Guillier, F. Allemand, C. Chiaruttini, and F. Dardel (2003)
J. Biol. Chem. 278, 36522-36530
   Abstract »    Full Text »    PDF »
Molecular dynamics reveals the stabilizing role of loop closing residues in kissing interactions: comparison between TAR-TAR* and TAR-aptamer.
F. Beaurain, C. Di Primo, J. J. Toulme, and M. Laguerre (2003)
Nucleic Acids Res. 31, 4275-4284
   Abstract »    Full Text »    PDF »
After the ribosome structures: How are the subunits assembled?.
J. R. WILLIAMSON (2003)
RNA 9, 165-167
   Abstract »    Full Text »    PDF »
Binding interactions between the core central domain of 16S rRNA and the ribosomal protein S15 determined by molecular dynamics simulations.
W. Li, B. Ma, and B. A. Shapiro (2003)
Nucleic Acids Res. 31, 629-638
   Abstract »    Full Text »    PDF »
The identification of spermine binding sites in 16S rRNA allows interpretation of the spermine effect on ribosomal 30S subunit functions.
I. Amarantos, I. K. Zarkadis, and D. L. Kalpaxis (2002)
Nucleic Acids Res. 30, 2832-2843
   Abstract »    Full Text »    PDF »
Mg2+-dependent conformational change of RNA studied by fluorescence correlation and FRET on immobilized single molecules.
H. D. Kim, G. U. Nienhaus, T. Ha, J. W. Orr, J. R. Williamson, and S. Chu (2002)
PNAS 99, 4284-4289
   Abstract »    Full Text »    PDF »
Crystal Structure of an Early Protein-RNA Assembly Complex of the Signal Recognition Particle.
K. Wild, I. Sinning, and S. Cusack (2001)
Science 294, 598-601
   Abstract »    Full Text »    PDF »
Recognition of RNA Branch Point Sequences by the KH Domain of Splicing Factor 1 (Mammalian Branch Point Binding Protein) in a Splicing Factor Complex.
H. Peled-Zehavi, J. A. Berglund, M. Rosbash, and A. D. Frankel (2001)
Mol. Cell. Biol. 21, 5232-5241
   Abstract »    Full Text »    PDF »
Protein-RNA interactions: a structural analysis.
S. Jones, D. T. A. Daley, N. M. Luscombe, H. M. Berman, and J. M. Thornton (2001)
Nucleic Acids Res. 29, 943-954
   Abstract »    Full Text »    PDF »
Straightening of bulged RNA by the double-stranded RNA-binding domain from the protein kinase PKR.
X. Zheng and P. C. Bevilacqua (2000)
PNAS
   Abstract »    Full Text »
Structure of Yeast Poly(A) Polymerase Alone and in Complex with 3'-dATP.
J. Bard, A. M. Zhelkovsky, S. Helmling, T. N. Earnest, C. L. Moore, and A. Bohm (2000)
Science 289, 1346-1349
   Abstract »    Full Text »
The Plastid Ribosomal Proteins. IDENTIFICATION OF ALL THE PROTEINS IN THE 30 S SUBUNIT OF AN ORGANELLE RIBOSOME (CHLOROPLAST).
K. Yamaguchi, K. von Knoblauch, and A. R. Subramanian (2000)
J. Biol. Chem. 275, 28455-28465
   Abstract »    Full Text »    PDF »
Straightening of bulged RNA by the double-stranded RNA-binding domain from the protein kinase PKR.
X. Zheng and P. C. Bevilacqua (2000)
PNAS 97, 14162-14167
   Abstract »    Full Text »    PDF »


ADVERTISEMENT
Click Me!

ADVERTISEMENT
Click Me!

To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)