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

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Stalled translation during elongation is an aberrant phenomenon during protein synthesis. Thus, once detected, it is subjected to quality control in which mRNA and a nascent protein are rapidly degraded. Although the mechanism of degradation for stalled translation is reasonably well understood, the initial processes, including those for detecting stalled translation, have not been determined. The ubiquitin proteasome pathway has been determined to function in the degradation of a nascent protein during stalled translation. Because a ubiquitin signal is one of the most versatile of cellular signals, we investigated the roles of various ubiquitination mechanisms in the budding yeast Saccharomyces cerevisiae using ubiquitin mutants that inhibited the polymerization of specific ubiquitin chains. We identified a role of non-proteasomal K63 polyubiquitination in stalled translation surveillance. Moreover, a K63R ubiquitin mutant barely inhibited the quality control pathway for nonstop translation, indicating distinct mechanisms for these highly related quality control pathways. These findings provide insights into the fundamental mechanisms for the initial processes of stalled translation surveillance and further emphasize the versatility of ubiquitin signals in cellular systems.

Vyšlo v časopise: Inhibiting K63 Polyubiquitination Abolishes No-Go Type Stalled Translation Surveillance in. PLoS Genet 11(4): e32767. doi:10.1371/journal.pgen.1005197
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.pgen.1005197

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