DOI: 10.1146/annurev.biophys.37.032807.125954. Ribosome Structure and Dynamics During Translocation and Termination

Ribosome Structure and Dynamics During Translocation and Termination

10.1146/annurev.biophys.37.032807.125954

Crossref journal-article

Annual Reviews

Annual Review of Biophysics (22)

Abstract

Protein biosynthesis, or translation, occurs on the ribosome, a large RNA-protein assembly universally conserved in all forms of life. Over the last decade, structures of the small and large ribosomal subunits and of the intact ribosome have begun to reveal the molecular details of how the ribosome works. Both cryo-electron microscopy and X-ray crystallography continue to provide fresh insights into the mechanism of translation. In this review, we describe the most recent structural models of the bacterial ribosome that shed light on the movement of messenger RNA and transfer RNA on the ribosome after each peptide bond is formed, a process termed translocation. We also discuss recent structures that reveal the molecular basis for stop codon recognition during translation termination. Finally, we review recent advances in understanding how bacteria handle errors in both translocation and termination.

Bibliography

Dunkle, J. A., & Cate, J. H. D. (2010). Ribosome Structure and Dynamics During Translocation and Termination. Annual Review of Biophysics, 39(1), 227â244.

Authors 2

Jack A. Dunkle (first)
Jamie H.D. Cate (additional)

References 96 Referenced 88

Dates

Type	When
Created	15 years, 3 months ago (May 12, 2010, 6:28 p.m.)
Deposited	3 years, 10 months ago (Oct. 6, 2021, 3:21 p.m.)
Indexed	2 months, 1 week ago (June 25, 2025, 5:07 p.m.)
Issued	15 years, 5 months ago (April 1, 2010)
Published	15 years, 5 months ago (April 1, 2010)
Published Print	15 years, 5 months ago (April 1, 2010)

Funders 0

None

BibTeX

@article{Dunkle_2010, title={Ribosome Structure and Dynamics During Translocation and Termination}, volume={39}, ISSN={1936-1238}, url={http://dx.doi.org/10.1146/annurev.biophys.37.032807.125954}, DOI={10.1146/annurev.biophys.37.032807.125954}, number={1}, journal={Annual Review of Biophysics}, publisher={Annual Reviews}, author={Dunkle, Jack A. and Cate, Jamie H.D.}, year={2010}, month=apr, pages={227–244} }

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  "abstract": "<jats:p> Protein biosynthesis, or translation, occurs on the ribosome, a large RNA-protein assembly universally conserved in all forms of life. Over the last decade, structures of the small and large ribosomal subunits and of the intact ribosome have begun to reveal the molecular details of how the ribosome works. Both cryo-electron microscopy and X-ray crystallography continue to provide fresh insights into the mechanism of translation. In this review, we describe the most recent structural models of the bacterial ribosome that shed light on the movement of messenger RNA and transfer RNA on the ribosome after each peptide bond is formed, a process termed translocation. We also discuss recent structures that reveal the molecular basis for stop codon recognition during translation termination. Finally, we review recent advances in understanding how bacteria handle errors in both translocation and termination. </jats:p>",
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