N-Myristoylation of the Rpt2 subunit of the yeast 26S proteasome is implicated in the subcellular compartment-specific protein quality control system.

摘要: Ubiquitination is the posttranslational modification of a protein by covalent attachment ubiquitin. Controlled proteolysis via ubiquitin-proteasome system (\UPS) alleviates cellular stress clearing misfolded proteins. In budding yeast, UPS within nucleus degrades nuclear proteins as well imported from cytoplasm. While predominantly localization yeast proteasome maintained importin-mediated transport, N-myristoylation subunit Rpt2 was indicated to cause dynamic nucleo-cytoplasmic proteasomes. Here, we quantitatively analyzed ubiquitinated peptides using anti-K-e-GG antibody in cell lines with or without mutation site and detected upregulated ubiquitination localizations mutant strains. Moreover, both peptide levels two Hsp70 family chaperones involved import proteins, Ssa Sse1, were elevated strains, whereas an chaperone export, Ssb, reduced. Taken together, our results indicate that controlled regulation proteasome.