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

X. Agirrezabala, E. Samatova, M. Macher, M. Liutkute, M. Maiti, D. Gil-Carton, J. Novacek, M. Valle, MV. Rodnina

. 2022 ; 41 (4) : e109175. [pub] 20220107

Language English Country Great Britain

Document type Journal Article, Research Support, Non-U.S. Gov't

Persistent link   https://www.medvik.cz/link/bmc22010995

Cellular proteins begin to fold as they emerge from the ribosome. The folding landscape of nascent chains is not only shaped by their amino acid sequence but also by the interactions with the ribosome. Here, we combine biophysical methods with cryo-EM structure determination to show that folding of a β-barrel protein begins with formation of a dynamic α-helix inside the ribosome. As the growing peptide reaches the end of the tunnel, the N-terminal part of the nascent chain refolds to a β-hairpin structure that remains dynamic until its release from the ribosome. Contacts with the ribosome and structure of the peptidyl transferase center depend on nascent chain conformation. These results indicate that proteins may start out as α-helices inside the tunnel and switch into their native folds only as they emerge from the ribosome. Moreover, the correlation of nascent chain conformations with reorientation of key residues of the ribosomal peptidyl-transferase center suggest that protein folding could modulate ribosome activity.

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$a Cellular proteins begin to fold as they emerge from the ribosome. The folding landscape of nascent chains is not only shaped by their amino acid sequence but also by the interactions with the ribosome. Here, we combine biophysical methods with cryo-EM structure determination to show that folding of a β-barrel protein begins with formation of a dynamic α-helix inside the ribosome. As the growing peptide reaches the end of the tunnel, the N-terminal part of the nascent chain refolds to a β-hairpin structure that remains dynamic until its release from the ribosome. Contacts with the ribosome and structure of the peptidyl transferase center depend on nascent chain conformation. These results indicate that proteins may start out as α-helices inside the tunnel and switch into their native folds only as they emerge from the ribosome. Moreover, the correlation of nascent chain conformations with reorientation of key residues of the ribosomal peptidyl-transferase center suggest that protein folding could modulate ribosome activity.
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$a Samatova, Ekaterina $u Department of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Gottingen, Germany $1 https://orcid.org/0000000175088076
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$a Macher, Meline $u Department of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Gottingen, Germany
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$a Maiti, Manisankar $u Department of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Gottingen, Germany $1 https://orcid.org/0000000266046971
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$a Novacek, Jiri $u CEITEC, Masaryk University, Brno, Czech Republic $1 https://orcid.org/0000000340133898
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$a Valle, Mikel $u CIC bioGUNE, Basque Research and Technology Alliance (BRTA), Derio, Spain $1 https://orcid.org/0000000182686912
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$a Rodnina, Marina V $u Department of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Gottingen, Germany $1 https://orcid.org/0000000301053879
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