Abstract
Rot1, an essential yeast protein, is degraded through the ER-associated protein degradation system (ERAD)
Highlights
Protein levels in cells are governed by protein synthesis and by protein degradation and is critical for maintaining cellular homeostasis
The ubiquitinproteasome system (UPS) constitutes the major mechanism by which cells acutely alter levels of cytosolic, nuclear, and endoplasmic reticulum (ER) proteins in a highly regulated manner [1, 2]. This occurs generally, but not exclusively, by conjugation with chains of ubiquitin linked through lysine 48 (K48) of ubiquitin, which targets modified proteins to the 26S proteasome for degradation [3, 4]
We found that Rot1 protein genetically weakly with Ubc1 [12]) and Doa10
Summary
Protein levels in cells are governed by protein synthesis and by protein degradation and is critical for maintaining cellular homeostasis. Same assays were performed using cell mutants in the pre pre subunits (components of the 20S which impact on the structure of the active site of the proteasome) and transformed with a plasmid containing the gene GAL1:ROT1HA. In contrast to WT cells, Rot protein levels poorly decay in the pre pre cells bearing the GAL1:ROT1-HA plasmid, persisting for more than 120 min after repression of the GAL promoter (Figure 1) This result confirmed that Rot is degraded through the ubiquitin proteasome system. We performed shut-off experiments in the three documented ubiquitin conjugating enzymes (E2s) yeast mutant cells (Ubc, Ubc and Ubc7) components of the ERAD pathway [2, 9] while expressing the plasmid containing the gene GAL1:ROT1-HA.
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