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.

Základní údaje

Originální název

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

Autoři

AGIRREZABALA, Xabier, Ekaterina SAMATOVA, Meline MACHER, Marija LIUTKUTE, Manisankar MAITI, David GIL-CARTON, Jiří NOVÁČEK (203 Česká republika, garant, domácí), Mikel VALLE a Marina V RODNINA

Vydání

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

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 11.400

Kód RIV

RIV/00216224:14740/22:00127878

Organizační jednotka

Středoevropský technologický institut

DOI

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

UT WoS

000739887500001

Klíčová slova anglicky

cotranslational folding; nascent chain; ribosome

Štítky

CF CRYO, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 18. 10. 2024 09:54, Ing. Jana Kuchtová

Anotace

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.

Návaznosti

90127, velká výzkumná infrastruktura

Název: CIISB II

Citovat

AGIRREZABALA, Xabier, Ekaterina SAMATOVA, Meline MACHER, Marija LIUTKUTE, Manisankar MAITI, David GIL-CARTON, Jiří NOVÁČEK, Mikel VALLE a Marina V RODNINA. A switch from alpha-helical to beta-strand conformation during co-translational protein folding. EMBO Journal. Hoboken (USA): WILEY-BLACKWELL, 2022, roč. 41, č. 4, s. 1-13. ISSN 0261-4189. Dostupné z: 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 a 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, roč.~41, č.~4, s.~1-13. ISSN~0261-4189. Dostupné z: https://dx.doi.org/10.15252/embj.2021109175.

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