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.
Science Signaling - Call For Papers

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 2 December 2005:
Vol. 310. no. 5753, pp. 1513 - 1515
DOI: 10.1126/science.1118977
Prev | Table of Contents | Next

Reports

Structural Roles for Human Translation Factor eIF3 in Initiation of Protein Synthesis

Bunpote Siridechadilok,1 Christopher S. Fraser,1,3* Richard J. Hall,4* Jennifer A. Doudna,1,2,3,4{dagger} Eva Nogales1,3,4{dagger}

Protein synthesis in mammalian cells requires initiation factor eIF3, a ~750-kilodalton complex that controls assembly of 40S ribosomal subunits on messenger RNAs (mRNAs) bearing either a 5'-cap or an internal ribosome entry site (IRES). Cryo–electron microscopy reconstructions show that eIF3, a five-lobed particle, interacts with the hepatitis C virus (HCV) IRES RNA and the 5'-cap binding complex eIF4F via the same domain. Detailed modeling of eIF3 and eIF4F onto the 40S ribosomal subunit reveals that eIF3 uses eIF4F or the HCV IRES in structurally similar ways to position the mRNA strand near the exit site of 40S, promoting initiation complex assembly.

1 Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.
2 Department of Chemistry, University of California, Berkeley, CA 94720, USA.
3 Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, USA.
4 Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.

* These authors contributed equally to this work.

{dagger} To whom correspondence should be addressed. E-mail: enogales{at}lbl.gov (E.N.); doudna{at}berkeley.edu (J.A.D.)

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Cap-dependent eukaryotic initiation factor-mRNA interactions probed by cross-linking.
L. Lindqvist, H. Imataka, and J. Pelletier (2008)
RNA 14, 960-969
   Abstract »    Full Text »    PDF »
The mechanism of an exceptional case of reinitiation after translation of a long ORF reveals why such events do not generally occur in mammalian mRNA translation.
T. A.A. Poyry, A. Kaminski, E. J. Connell, C. S. Fraser, and R. J. Jackson (2007)
Genes & Dev. 21, 3149-3162
   Abstract »    Full Text »    PDF »
Targeted inhibition of the hepatitis C internal ribosomal entry site genomic RNA with oligonucleotide conjugates.
V. Guerniou, R. Gillet, F. Berree, B. Carboni, and B. Felden (2007)
Nucleic Acids Res. 35, 6778-6787
   Abstract »    Full Text »    PDF »
Studying Hepatitis C Virus: Making the Best of a Bad Virus.
T. L. Tellinghuisen, M. J. Evans, T. von Hahn, S. You, and C. M. Rice (2007)
J. Virol. 81, 8853-8867
   Full Text »    PDF »
Novel activity of eukaryotic translocase, eEF2: dissociation of the 80S ribosome into subunits with ATP but not with GTP.
N. Demeshkina, G. Hirokawa, A. Kaji, and H. Kaji (2007)
Nucleic Acids Res. 35, 4597-4607
   Abstract »    Full Text »    PDF »
A search for structurally similar cellular internal ribosome entry sites.
S. D. Baird, S. M. Lewis, M. Turcotte, and M. Holcik (2007)
Nucleic Acids Res. 35, 4664-4677
   Abstract »    Full Text »    PDF »
Structural Characterization of the Human Eukaryotic Initiation Factor 3 Protein Complex by Mass Spectrometry.
E. Damoc, C. S. Fraser, M. Zhou, H. Videler, G. L. Mayeur, J. W. B. Hershey, J. A. Doudna, C. V. Robinson, and J. A. Leary (2007)
Mol. Cell. Proteomics 6, 1135-1146
   Abstract »    Full Text »    PDF »
Translation factor control of ribosome conformation during start codon selection.
K. Asano and M. S. Sachs (2007)
Genes & Dev. 21, 1280-1287
   Full Text »    PDF »
Reconfiguration of yeast 40S ribosomal subunit domains by the translation initiation multifactor complex.
R. J. C. Gilbert, Y. Gordiyenko, T. von der Haar, A. F.-P. Sonnen, G. Hofmann, M. Nardelli, D. I. Stuart, and J. E. G. McCarthy (2007)
PNAS 104, 5788-5793
   Abstract »    Full Text »    PDF »
Structure of eIF3b RNA Recognition Motif and Its Interaction with eIF3j: STRUCTURAL INSIGHTS INTO THE RECRUITMENT OF eIF3b TO THE 40 S RIBOSOMAL SUBUNIT.
L. ElAntak, A. G. Tzakos, N. Locker, and P. J. Lukavsky (2007)
J. Biol. Chem. 282, 8165-8174
   Abstract »    Full Text »    PDF »
Rabies virus matrix protein interplay with eIF3, new insights into rabies virus pathogenesis.
A. V. Komarova, E. Real, A. M. Borman, M. Brocard, P. England, N. Tordo, J. W.B. Hershey, K. M. Kean, and Y. Jacob (2007)
Nucleic Acids Res. 35, 1522-1532
   Abstract »    Full Text »    PDF »
Individual Overexpression of Five Subunits of Human Translation Initiation Factor eIF3 Promotes Malignant Transformation of Immortal Fibroblast Cells.
L. Zhang, X. Pan, and J. W. B. Hershey (2007)
J. Biol. Chem. 282, 5790-5800
   Abstract »    Full Text »    PDF »
Oscillating kissing stem-loop interactions mediate 5' scanning-dependent translation by a viral 3'-cap-independent translation element.
A. M. Rakotondrafara, C. Polacek, E. Harris, and W. A. Miller (2006)
RNA 12, 1893-1906
   Abstract »    Full Text »    PDF »
Searching for IRES.
S. D. Baird, M. Turcotte, R. G. Korneluk, and M. Holcik (2006)
RNA 12, 1755-1785
   Abstract »    Full Text »    PDF »
Translation Initiation Factor eIF4G-1 Binds to eIF3 through the eIF3e Subunit.
A. K. LeFebvre, N. L. Korneeva, M. Trutschl, U. Cvek, R. D. Duzan, C. A. Bradley, J. W. B. Hershey, and R. E. Rhoads (2006)
J. Biol. Chem. 281, 22917-22932
   Abstract »    Full Text »    PDF »
From Structure to Function: New Insights into Hepatitis C Virus RNA Replication.
N. Appel, T. Schaller, F. Penin, and R. Bartenschlager (2006)
J. Biol. Chem. 281, 9833-9836
   Full Text »    PDF »


ADVERTISEMENT
Click Me!

ADVERTISEMENT
Click Me!

To Advertise     Find Products

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