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  A switch from α‐helical to β‐strand conformation during co‐translational protein folding

Agirrezabala, X., Samatova, E., Macher, M., Liutkute, M., Maiti, M., Gil‐Carton, D., et al. (2022). A switch from α‐helical to β‐strand conformation during co‐translational protein folding. The EMBO Journal, 41(4): e109175. doi:10.15252/embj.2021109175.

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Agirrezabala, X., Author
Samatova, E.1, Author                 
Macher, M., Author
Liutkute, M.1, Author                 
Maiti, M.1, Author                 
Gil‐Carton, D., Author
Novacek, J., Author
Valle, M., 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: cotranslational folding; nascent chain; ribosome
 Abstract: Cellular proteins begin to fold as they emerge from the ribosome.The folding landscape of nascent chains is not only shaped by theiramino acid sequence but also by the interactions with the ribo-some. Here, we combine biophysical methods with cryo-EM struc-ture determination to show that folding of aβ-barrel proteinbegins with formation of a dynamicα-helix inside the ribosome. Asthe growing peptide reaches the end of the tunnel, the N-terminalpart of the nascent chain refolds to aβ-hairpin structure thatremains dynamic until its release from the ribosome. Contactswith the ribosome and structure of the peptidyl transferase centerdepend on nascent chain conformation. These results indicate thatproteins may start out asα-helices inside the tunnel and switchinto their native folds only as they emerge from the ribosome.Moreover, the correlation of nascent chain conformations withreorientation of key residues of the ribosomal peptidyl-transferasecenter suggest that protein folding could modulate ribosome activity.

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Language(s): eng - English
 Dates: 2022-01-072022-02-15
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.15252/embj.2021109175
 Degree: -

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Project name : RIBOFOLD
Grant ID : 787926
Funding program : Ribosome Processivity and Co-translational Protein Folding
Funding organization : European Commission (EC)
Project name : The work was funded by the Max Planck Society to M.V.R., the European Research Council (ERC) Advanced Investigator Grant RIBOFOLD to M.V.R. (proposal number n° 787926), and the Spanish Ministry of Economy and Competitiveness to X.A. (CTQ2015-73560-JIN) and to M.V. (PGC2018-098996-B-I00). We thank the Spanish Ministry of Science for the Severo Ochoa Excellence Accreditations to the CIC bioGUNE (SEV-2016-0644). CIISB research infrastructure project LM2018127 funded by MEYS CR is gratefully acknowledged for the financial support of the measurements at the CF Cryo-electron Microscopy and Tomography. Open Access funding enabled and organized by Projekt DEAL.
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Title: The EMBO Journal
Source Genre: Journal
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Pages: 13 Volume / Issue: 41 (4) Sequence Number: e109175 Start / End Page: - Identifier: ISSN: 0261-4189
ISSN: 1460-2075