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The type‐2 N‐end rule peptide recognition activity of Ubr11 ubiquitin ligase is required for the expression of peptide transporters
Author(s) -
Kitamura Kenji,
Fujiwara Hidenobu
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.11.028
Subject(s) - ubiquitin ligase , peptide , ubiquitin , chemistry , microbiology and biotechnology , dna ligase , biochemistry , biology , gene
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.