QUALITY CONTROL OF PROTEIN FOLDING
CHAN SHU NING
CHAN SHU NING
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Abstract
Cytosolic protein quality control (CytoQC) consists of a robust network of components that monitor the integrity of protein folding and degradation. Aberrant proteins arising from misfolding or mis-localization are promptly eliminated by the CytoQC machinery to protect the cell from potential toxicity. Nevertheless, a comprehensive map of the components involved is still lacking. The complexity of the CytoQC network and diversity of clients suggest there are yet-identified components in this pathway. In this study, I established an unbiased, genome-wide selection to identify new components of CytoQC. Spontaneously-occurring CytoQC-defective mutants were isolated based on the observation of uracil prototrophic growth in cells expressing a novel reporter. I have identified Ubr1, a known CytoQC E3 ligase, and six new candidates of CytoQC including the proteasomal subunit Pup2 and deubiquitinase Doa4. Characterization of these two candidates validated the usefulness of the selection and revealed new knowledge on the selectivity and sensitivity of CytoQC.
Keywords
protein quality control, genetic selection, cytosol, spontaneous mutations, proteasome, deubiquitinase
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2019-08-16
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