Protein Knotting by Active Threading of Nascent Polypeptide Chain Exiting from the Ribosome Exit Channel.

Détails

ID Serval
serval:BIB_5A109FDEE6B9
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Protein Knotting by Active Threading of Nascent Polypeptide Chain Exiting from the Ribosome Exit Channel.
Périodique
The journal of Physical Chemistry. B
Auteur(s)
Dabrowski-Tumanski P., Piejko M., Niewieczerzal S., Stasiak A., Sulkowska J.I.
ISSN
1520-5207 (Electronic)
ISSN-L
1520-5207
Statut éditorial
Publié
Date de publication
2018
Peer-reviewed
Oui
Volume
122
Numéro
49
Pages
11616-11625
Langue
anglais
Résumé
The mechanism of folding of deeply knotted proteins into their native structure is still not understood. Current thinking about protein folding is dominated by the Anfinsen dogma, stating that the structure of the folded proteins is uniquely dictated by the amino acid sequence of a given protein and that the folding is driven uniquely by the energy gained from interactions between amino acids that contact each other in the native structure of the protein. The role of ribosomes in protein folding was only seen as permitting the folding to progress from the N-terminal part of nascent protein chains. We propose here that ribosomes can participate actively in the folding of knotted proteins by actively threading nascent chains emerging from the ribosome exit channels through loops formed by a synthesized earlier portion of the same protein. Our simulations of folding of deeply knotted protein Tp0624 positively verify the proposed ribosome-driven active threading mechanism leading to the formation of deeply knotted proteins.
Pubmed
Web of science
Création de la notice
05/11/2018 9:14
Dernière modification de la notice
20/08/2019 14:13
Données d'usage