Skip to main content
×
Home
    • Aa
    • Aa

Elongation in translation as a dynamic interaction among the ribosome, tRNA, and elongation factors EF-G and EF-Tu

  • Xabier Agirrezabala (a1) and Joachim Frank (a1) (a2)
Abstract
Abstract

The ribosome is a complex macromolecular machine that translates the message encoded in the messenger RNA and synthesizes polypeptides by linking the individual amino acids carried by the cognate transfer RNAs (tRNAs). The protein elongation cycle, during which the tRNAs traverse the ribosome in a coordinated manner along a path of more than 100 Å, is facilitated by large-scale rearrangements of the ribosome. These rearrangements go hand in hand with conformational changes of tRNA as well as elongation factors EF-Tu and EF-G – GTPases that catalyze tRNA delivery and translocation, respectively. This review focuses on the structural data related to the dynamics of the ribosomal machinery, which are the basis, in conjunction with existing biochemical, kinetic, and fluorescence resonance energy transfer data, of our knowledge of the decoding and translocation steps of protein elongation.

Copyright
Corresponding author
*Author for correspondence: Dr. J. Frank, The Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University, P&S BB 2-221, 650 West 168th Street, New York, NY 10032, USA. Email: jf2192@columbia.edu
Linked references
Hide All

This list contains references from the content that can be linked to their source. For a full set of references and notes please see the PDF or HTML where available.

H. Gao , J. Lebarron & J. Frank (2009). Ribosomal dynamics: intrinsic instability of a molecular machine. In Non-Protein Coding RNAs (eds. N. G. Walter , S. A. Woodson & R. T. Batey ), pp 303316. Berlin: Springer-Verlag.

J. Lebarron , K. Mitra & J. Frank (2007). Displaying 3D data on RNA secondary structures: ColoRNA. Journal of Structural Biology 157, 262270.

J. Lebarron , R. A. Grassucci , T. R. Shaikh , W. T. Baxter , J. Sengupta & J. Frank (2008). Exploration of parameters in cryo-EM leading to an improved density map of the E. coli ribosome. Journal of Structural Biology 164, 2432.

R. Lill , J. M. Robertson & W. Wintermeyer (1989). Binding of the 3′ terminus of tRNA to 23S rRNA in the ribosomal exit site actively promotes translocation. EMBO Journal 8, 39333938.

Recommend this journal

Email your librarian or administrator to recommend adding this journal to your organisation's collection.

Quarterly Reviews of Biophysics
  • ISSN: 0033-5835
  • EISSN: 1469-8994
  • URL: /core/journals/quarterly-reviews-of-biophysics
Please enter your name
Please enter a valid email address
Who would you like to send this to? *
×

Metrics

Altmetric attention score

Full text views

Total number of HTML views: 6
Total number of PDF views: 18 *
Loading metrics...

Abstract views

Total abstract views: 188 *
Loading metrics...

* Views captured on Cambridge Core between September 2016 - 23rd September 2017. This data will be updated every 24 hours.