Protein Elongation, Co-translational Folding and Targeting
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- 作者：Marina V. Rodnina ; rodnina@mpibpc.mpg.de" class="auth_mail" title="E-mail the corresponding author ; Wolfgang Wintermeyer ; wolfgang.wintermeyer@mpibpc.mpg.de" class="auth_mail" title="E-mail the corresponding author
- 关键词：EF ; elongation factor ; aa-tRNA ; aminoacyl-tRNA ; rRNA ; ribosomal RNA ; SRL ; sarcin-ricin loop ; SSU ; small subunit of the ribosome ; LSU ; large subunit of the ribosome ; TS ; transition state ; cryo-EM ; cryo-electron microscopy ; PRF ; programmed ribosome frameshifting ; RPB ; ribosome-associated protein biogenesis factor ; TF ; trigger factor ; SRP ; signal recognition particle ; PDF ; peptide deformylase ; MAP ; methionine aminopeptidase ; RNC ; ribosome-nascent-chain complex ; SAS ; signal-anchor sequence ; TM ; tran
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：22 May 2016
- 年：2016
- 卷：428
- 期：10
- 页码：2165-2185
- 全文大小：2012 K
文摘
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Ribosome dynamics control decoding and translocation.
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A specialized translation factor is required for the synthesis of proline stretches.
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Programmed ribosome frameshifting is due to impeded translocation.
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The ribosomal peptide exit tunnel directs co-translational protein folding.
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The translocon opens laterally on ribosome binding and signal peptide insertion.