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

Published online by Cambridge University Press:  22 December 2009

Xabier Agirrezabala  and
Joachim Frank
Xabier Agirrezabala
Affiliation:
The Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, USA
Joachim Frank*
Affiliation:
The Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, USA Department of Biological Sciences, Columbia University, New York, NY, USA
*
*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
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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.

Type
Review Article
Information
Quarterly Reviews of Biophysics , Volume 42 , Issue 3 , August 2009 , pp. 159 - 200
Copyright
Copyright © Cambridge University Press 2009

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