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  Lateral gate dynamics of the bacterial translocon during cotranslational membrane protein insertion

Mercier, E., Wang, X., Maiti, M., Wintermeyer, W., & Rodnina, M. V. (2021). Lateral gate dynamics of the bacterial translocon during cotranslational membrane protein insertion. Proceedings of the National Academy of Sciences of the USA, 118(26): e2100474118. doi:10.1073/pnas.2100474118.

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 Creators:
Mercier, E.1, Author              
Wang, X.1, Author              
Maiti, M.1, Author              
Wintermeyer, W.2, Author              
Rodnina, M. V.3, Author              
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              
3Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578598              

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Free keywords: single-molecule biophysics; YidC; membrane proteins; ribosome; translocon SecYEG
 Abstract: During synthesis of membrane proteins, transmembrane segments (TMs) of nascent proteins emerging from the ribosome are inserted into the central pore of the translocon (SecYEG in bacteria) and access the phospholipid bilayer through the open lateral gate formed of two helices of SecY. Here we use single-molecule fluorescence resonance energy transfer to monitor lateral-gate fluctuations in SecYEG embedded in nanodiscs containing native membrane phospholipids. We find the lateral gate to be highly dynamic, sampling the whole range of conformations between open and closed even in the absence of ligands, and we suggest a statistical model-free approach to evaluate the ensemble dynamics. Lateral gate fluctuations take place on both short (submillisecond) and long (subsecond) timescales. Ribosome binding and TM insertion do not halt fluctuations but tend to increase sampling of the open state. When YidC, a constituent of the holotranslocon, is bound to SecYEG, TM insertion facilitates substantial opening of the gate, which may aid in the folding of YidC-dependent polytopic membrane proteins. Mutations in lateral gate residues showing in vivo phenotypes change the range of favored states, underscoring the biological significance of lateral gate fluctuations. The results suggest how rapid fluctuations of the lateral gate contribute to the biogenesis of inner-membrane proteins.

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Language(s): eng - English
 Dates: 2021-06-232021-06-29
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1073/pnas.2100474118
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Title: Proceedings of the National Academy of Sciences of the USA
Source Genre: Journal
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Pages: 8 Volume / Issue: 118 (26) Sequence Number: e2100474118 Start / End Page: - Identifier: -