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Avr 26 2016

Imprimer ce Article

Protein elongation, co-translational folding and targeting

Journal

J Mol Biol. 2016 Mar 30. pii: S0022-2836(16)30001-8. doi: 10.1016/j.jmb.2016.03.022. [Epub ahead of print]

Authors

Rodnina MV, Wintermeyer W.

Abstract

The elongation phase of protein synthesis defines the overall speed and fidelity of protein synthesis and affects protein folding and targeting. The mechanisms of reactions taking place during translation elongation remain important questions in understanding ribosome function. The ribosome – guided by signals in the mRNA – can recode the genetic information, resulting in alternative protein products. Co-translational protein folding and interaction of ribosomes and emerging polypeptides with associated protein biogenesis factors determines the quality and localization of proteins. In this review we summarize recent findings on mechanisms of translation elongation in bacteria, including decoding and recoding, peptide bond formation, tRNA-mRNA translocation, co-translational protein folding, interaction with protein biogenesis factors, and targeting of ribosomes synthesizing membrane proteins to the plasma membrane. The data provide insights into how the ribosome shapes composition and quality of the cellular proteome.

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