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  Protein elongation, co-translational folding and targeting.

Rodnina, M. V., & Wintermeyer, W. (2016). Protein elongation, co-translational folding and targeting. Journal of Molecular Biology, 428(10, P. B), 2165-2185. doi:10.1016/j.jmb.2016.03.022.

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 Urheber:
Rodnina, M. V.1, Autor           
Wintermeyer, W.2, Autor           
Affiliations:
1Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578598              
2Research Group of Ribosome Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578599              

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Schlagwörter: membrane targeting; protein folding; recoding; ribosome; translation factors
 Zusammenfassung: 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 determine 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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Sprache(n): eng - English
 Datum: 2016-03-302016-05-22
 Publikationsstatus: Erschienen
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 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1016/j.jmb.2016.03.022
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Titel: Journal of Molecular Biology
Genre der Quelle: Zeitschrift
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Seiten: - Band / Heft: 428 (10, P. B) Artikelnummer: - Start- / Endseite: 2165 - 2185 Identifikator: -