Accéder directement au contenu Accéder directement à la navigation
Article dans une revue

Structure of UBE2Z Enzyme Provides Functional Insight into Specificity in the FAT10 Protein Conjugation Machinery

Abstract : FAT10 conjugation, a post-translational modification analogous to ubiquitination, specifically requires UBA6 and UBE2Z as its activating (E1) and conjugating (E2) enzymes. Interestingly, these enzymes can also function in ubiquitination. We have determined the crystal structure of UBE2Z and report how the different domains of this E2 enzyme are organized. We further combine our structural data with mutational analyses to understand how specificity is achieved in the FAT10 conjugation pathway. We show that specificity toward UBA6 and UBE2Z lies within the C-terminal CYCI tetrapeptide in FAT10. We also demonstrate that this motif slows down transfer rates for FAT10 from UBA6 onto UBE2Z.
Type de document :
Article dans une revue
Liste complète des métadonnées

https://hal.univ-lille.fr/hal-03182082
Contributeur : Lilloa Université de Lille <>
Soumis le : vendredi 26 mars 2021 - 10:23:09
Dernière modification le : samedi 27 mars 2021 - 03:32:01
Archivage à long terme le : : dimanche 27 juin 2021 - 18:24:12

Fichier

PIIS0021925820361962.pdf
Fichiers produits par l'(les) auteur(s)

Licence


Distributed under a Creative Commons Paternité 4.0 International License

Identifiants

Collections

Citation

Julien Schelpe, Didier Monte, Frederique Dewitte, Titia K. Sixma, Prakash Rucktooa. Structure of UBE2Z Enzyme Provides Functional Insight into Specificity in the FAT10 Protein Conjugation Machinery. The Journal of biological chemistry, 2016, The Journal of biological chemistry, 291 (2), pp.630-639. ⟨10.1074/jbc.M115.671545⟩. ⟨hal-03182082⟩

Partager

Métriques

Consultations de la notice

22

Téléchargements de fichiers

27