mRNA-programmed translation pauses in the targeting of E. coli membrane proteins

In all living organisms, ribosomes translating membrane proteins are targeted to membrane translocons early in translation, by the ubiquitous signal recognition particle (SRP) system. In eukaryotes, the SRP Alu domain arrests translation elongation of membrane proteins until targeting is complete. C...

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Main Authors: Nir Fluman, Sivan Navon, Eitan Bibi, Yitzhak Pilpel
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2014-08-01
Series:eLife
Subjects:
Online Access:https://elifesciences.org/articles/03440
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spelling doaj-364ccf0da3bf4d2ba8b7b9b272dd01252021-05-04T23:25:11ZengeLife Sciences Publications LtdeLife2050-084X2014-08-01310.7554/eLife.03440mRNA-programmed translation pauses in the targeting of E. coli membrane proteinsNir Fluman0Sivan Navon1Eitan Bibi2Yitzhak Pilpel3Department of Molecular Genetics, Weizmann Institute of Science, Rehovot, IsraelDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot, IsraelDepartment of Biological Chemistry, Weizmann Institute of Science, Rehovot, IsraelDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot, IsraelIn all living organisms, ribosomes translating membrane proteins are targeted to membrane translocons early in translation, by the ubiquitous signal recognition particle (SRP) system. In eukaryotes, the SRP Alu domain arrests translation elongation of membrane proteins until targeting is complete. Curiously, however, the Alu domain is lacking in most eubacteria. In this study, by analyzing genome-wide data on translation rates, we identified a potential compensatory mechanism in E. coli that serves to slow down the translation during membrane protein targeting. The underlying mechanism is likely programmed into the coding sequence, where Shine–Dalgarno-like elements trigger elongation pauses at strategic positions during the early stages of translation. We provide experimental evidence that slow translation during targeting and improves membrane protein production fidelity, as it correlates with better folding of overexpressed membrane proteins. Thus, slow elongation is important for membrane protein targeting in E. coli, which utilizes mechanisms different from the eukaryotic one to control the translation speed.https://elifesciences.org/articles/03440membrane proteintranslation ratequality control
collection DOAJ
language English
format Article
sources DOAJ
author Nir Fluman
Sivan Navon
Eitan Bibi
Yitzhak Pilpel
spellingShingle Nir Fluman
Sivan Navon
Eitan Bibi
Yitzhak Pilpel
mRNA-programmed translation pauses in the targeting of E. coli membrane proteins
eLife
membrane protein
translation rate
quality control
author_facet Nir Fluman
Sivan Navon
Eitan Bibi
Yitzhak Pilpel
author_sort Nir Fluman
title mRNA-programmed translation pauses in the targeting of E. coli membrane proteins
title_short mRNA-programmed translation pauses in the targeting of E. coli membrane proteins
title_full mRNA-programmed translation pauses in the targeting of E. coli membrane proteins
title_fullStr mRNA-programmed translation pauses in the targeting of E. coli membrane proteins
title_full_unstemmed mRNA-programmed translation pauses in the targeting of E. coli membrane proteins
title_sort mrna-programmed translation pauses in the targeting of e. coli membrane proteins
publisher eLife Sciences Publications Ltd
series eLife
issn 2050-084X
publishDate 2014-08-01
description In all living organisms, ribosomes translating membrane proteins are targeted to membrane translocons early in translation, by the ubiquitous signal recognition particle (SRP) system. In eukaryotes, the SRP Alu domain arrests translation elongation of membrane proteins until targeting is complete. Curiously, however, the Alu domain is lacking in most eubacteria. In this study, by analyzing genome-wide data on translation rates, we identified a potential compensatory mechanism in E. coli that serves to slow down the translation during membrane protein targeting. The underlying mechanism is likely programmed into the coding sequence, where Shine–Dalgarno-like elements trigger elongation pauses at strategic positions during the early stages of translation. We provide experimental evidence that slow translation during targeting and improves membrane protein production fidelity, as it correlates with better folding of overexpressed membrane proteins. Thus, slow elongation is important for membrane protein targeting in E. coli, which utilizes mechanisms different from the eukaryotic one to control the translation speed.
topic membrane protein
translation rate
quality control
url https://elifesciences.org/articles/03440
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