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- Title
The type-2 N-end rule peptide recognition activity of Ubr11 ubiquitin ligase is required for the expression of peptide transporters
- Authors
Kitamura, Kenji; Fujiwara, Hidenobu
- Abstract
Abstract: The Ubr1-like canonical N-recognins, widely conserved ubiquitin ligases in eukaryotes, play a role in the N-end rule pathway-mediated degradation of substrates harboring basic (type-1) or bulky hydrophobic (type-2) amino acids at the N-terminus. In this study, the roles of conserved domains were studied in the Schizosaccharomyces pombe Ubr11 protein. Mutations in the UBR box and the autoinhibitory domain blocked degradation of both type-1 and type-2 substrates, expression of peptide transporter genes, and the uptake of oligopeptides. An N-domain mutant was normal for the type-1-related function, but nevertheless failed to express peptide transporters. These data suggest the importance of the type-2-related activity of Ubr11 for its in vivo function.
- Subjects
UBIQUITIN ligases; SCHIZOSACCHAROMYCES; GENE expression; CARRIER proteins; EUKARYOTES; GENETIC mutation; MUTANT proteins
- Publication
FEBS Letters, 2013, Vol 587, Issue 2, p214
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2012.11.028