The type-2 N-end rule peptide recognition activity of Ubr11 ubiquitin ligase is required for the expression of peptide transporters

作者：Kitamura Kenji^*; Fujiwara Hidenobu

来源：FEBS Letters, 2013, 587(2): 214-219.

DOI：10.1016/j.febslet.2012.11.028

• N-end rule pathway
• N-recognin
• UBR protein
• N-degron
• Dipeptide
• Schizosaccharomyces pombe

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.

• 出版日期2013-1-16