Inhibiting K63 Polyubiquitination Abolishes No-Go Type Stalled Translation Surveillance in Saccharomyces cerevisiae

• DOI: 10.1371/journal.pgen.1005197
• Publication Date: 2015-04-24T18:04:48Z
• Authors: Kazuki Saito; Wataru Horikawa; Koichi Ito
• Keywords: Ubiquitin-Protein Ligases; Protein Degradation; Deubiquitinating enzyme; Ribosome profiling

Incidental ribosome stalling during translation elongation is an aberrant phenomenon protein synthesis and subjected to quality control by surveillance systems, in which mRNA a nascent are rapidly degraded. Their detailed molecular mechanisms as well responsible factors for these processes beginning be understood. However, the initial detecting stalled that result degradation remain determined. Among identified date, two E3 ubiquitin ligases have been reported function distinct manners. Because ubiquitination one of most versatile cellular signals, functions suggested diverse pathways translation. In this study, we report experimental evidences unique role non-proteasomal K63 polyubiquitination Inhibiting expressing K63R mutation Saccharomyces cerevisiae cells markedly abolished responses More analyses indicated effects mutants were independent proteasome dependent on Hel2, ligases. Moreover, mutant barely inhibited pathway nonstop translation, indicating highly related pathways. Our results suggest included process presumably triggers steps upon translational stall. These findings provide crucial information regarding involved systems their classification.