A switch from alpha-helical to beta-strand conformation during
co-translational protein folding

J 2022

A switch from alpha-helical to beta-strand conformation during co-translational protein folding

AGIRREZABALA, Xabier, Ekaterina SAMATOVA, Meline MACHER, Marija LIUTKUTE, Manisankar MAITI et. al.

Basic information

Original name

A switch from alpha-helical to beta-strand conformation during co-translational protein folding

Authors

AGIRREZABALA, Xabier, Ekaterina SAMATOVA, Meline MACHER, Marija LIUTKUTE, Manisankar MAITI, David GIL-CARTON, Jiří NOVÁČEK (203 Czech Republic, guarantor, belonging to the institution), Mikel VALLE and Marina V RODNINA

Edition

EMBO Journal, Hoboken (USA), WILEY-BLACKWELL, 2022, 0261-4189

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 11.400

RIV identification code

RIV/00216224:14740/22:00127878

Organization unit

Central European Institute of Technology

DOI

http://dx.doi.org/10.15252/embj.2021109175

UT WoS

000739887500001

Keywords in English

cotranslational folding; nascent chain; ribosome

Abstract

V originále

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.

Links

90127, large research infrastructures

Name: CIISB II

Citovat

AGIRREZABALA, Xabier, Ekaterina SAMATOVA, Meline MACHER, Marija LIUTKUTE, Manisankar MAITI, David GIL-CARTON, Jiří NOVÁČEK, Mikel VALLE and Marina V RODNINA. A switch from alpha-helical to beta-strand conformation during co-translational protein folding. EMBO Journal. Hoboken (USA): WILEY-BLACKWELL, 2022, vol. 41, No 4, p. 1-13. ISSN 0261-4189. Available from: https://dx.doi.org/10.15252/embj.2021109175.

@article{2245518,
   author = {Agirrezabala, Xabier and Samatova, Ekaterina and Macher, Meline and Liutkute, Marija and Maiti, Manisankar and GilandCarton, David and Nováček, Jiří and Valle, Mikel and Rodnina, Marina V},
   article_location = {Hoboken (USA)},
   article_number = {4},
   doi = {http://dx.doi.org/10.15252/embj.2021109175},
   keywords = {cotranslational folding; nascent chain; ribosome},
   language = {eng},
   issn = {0261-4189},
   journal = {EMBO Journal},
   title = {A switch from alpha-helical to beta-strand conformation during co-translational protein folding},
   url = {https://www.embopress.org/doi/full/10.15252/embj.2021109175},
   volume = {41},
   year = {2022}
}

TY  - JOUR
ID  - 2245518
AU  - Agirrezabala, Xabier - Samatova, Ekaterina - Macher, Meline - Liutkute, Marija - Maiti, Manisankar - Gil-Carton, David - Nováček, Jiří - Valle, Mikel - Rodnina, Marina V
PY  - 2022
TI  - A switch from alpha-helical to beta-strand conformation during co-translational protein folding
JF  - EMBO Journal
VL  - 41
IS  - 4
SP  - 1-13
EP  - 1-13
PB  - WILEY-BLACKWELL
SN  - 02614189
KW  - cotranslational folding
KW  - nascent chain
KW  - ribosome
UR  - https://www.embopress.org/doi/full/10.15252/embj.2021109175
N2  - 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.
ER  -

AGIRREZABALA, Xabier, Ekaterina SAMATOVA, Meline MACHER, Marija LIUTKUTE, Manisankar MAITI, David GIL-CARTON, Jiří NOVÁČEK, Mikel VALLE and Marina V RODNINA. A switch from alpha-helical to beta-strand conformation during co-translational protein folding. \textit{EMBO Journal}. Hoboken (USA): WILEY-BLACKWELL, 2022, vol.~41, No~4, p.~1-13. ISSN~0261-4189. Available from: https://dx.doi.org/10.15252/embj.2021109175.

Detailed Information on Publication Record