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  Cotranslational biogenesis of membrane proteins in bacteria

Mercier, E., Wang, X., Bögeholz, L. A. K., Wintermeyer, W., & Rodnina, M. V. (2022). Cotranslational biogenesis of membrane proteins in bacteria. Frontiers in Molecular Biosciences, 9: 871121. doi:10.3389/fmolb.2022.871121.

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 Creators:
Mercier, E.1, Author           
Wang, X.1, Author           
Bögeholz, L. A. K.1, Author           
Wintermeyer, W.1, Author           
Rodnina, M. V.1, Author           
Affiliations:
1Department of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society, ou_3350156              

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Free keywords: N-terminal processing, membrane targeting, membrane insertion, membrane protein topology, translocon, cotranslational folding, YidC
 Abstract: Nascent polypeptides emerging from the ribosome during translation are rapidly scanned and processed by ribosome-associated protein biogenesis factors (RPBs). RPBs cleave
the N-terminal formyl and methionine groups, assist cotranslational protein folding, and
sort the proteins according to their cellular destination. Ribosomes translating inner-
membrane proteins are recognized and targeted to the translocon with the help of the
signal recognition particle, SRP, and SRP receptor, FtsY. The growing nascent peptide is
then inserted into the phospholipid bilayer at the translocon, an inner-membrane protein
complex consisting of SecY, SecE, and SecG. Folding of membrane proteins requires that
transmembrane helices (TMs) attain their correct topology, the soluble domains are
inserted at the correct (cytoplasmic or periplasmic) side of the membrane, and – for
polytopic membrane proteins – the TMs find their interaction partner TMs in the
phospholipid bilayer. This review describes the recent progress in understanding how
growing nascent peptides are processed and how inner-membrane proteins are targeted
to the translocon and find their correct orientation at the membrane, with the focus on
biophysical approaches revealing the dynamics of the process. We describe how
spontaneous fluctuations of the translocon allow diffusion of TMs into the phospholipid
bilayer and argue that the ribosome orchestrates cotranslational targeting not only by
providing the binding platform for the RPBs or the translocon, but also by helping the
nascent chains to find their correct orientation in the membrane. Finally, we present the
auxiliary role of YidC as a chaperone for inner-membrane proteins. We show how
biophysical approaches provide new insights into the dynamics of membrane protein
biogenesis and raise new questions as to how translation modulates protein folding.

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Language(s): eng - English
 Dates: 2022-04-29
 Publication Status: Published online
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.3389/fmolb.2022.871121
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Project name : SFB1190
Grant ID : -
Funding program : -
Funding organization : DFG
Project name : -
Grant ID : 787926
Funding program : Advanced Investigator Grant RIBOFOLD
Funding organization : ERC
Project name : Germany’s Excellence Strategy
Grant ID : EXC 2067/1- 39072994
Funding program : -
Funding organization : -

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Title: Frontiers in Molecular Biosciences
Source Genre: Journal
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Pages: 15 Volume / Issue: 9 Sequence Number: 871121 Start / End Page: - Identifier: ISSN: 2296-889X