In contrast to the myriad approaches available to study protein misfolding and aggregation in vitro, relatively few tools are available for the study of these processes in the cellular context. This is in part due to the complexity of the cellular environment, which, for instance, interferes with many spectroscopic approaches. Here, we describe a tripartite fusion approach that can be used to assess in vivo protein stability and solubility in the cytosol of Saccharomyces cerevisiae. Our biosensors contain tripartite fusions in which a protein of interest is inserted into antibiotic resistance markers. These fusions act to directly link the aggregation susceptibility and stability of the inserted protein to antibiotic resistance. We demonstrate a linear relationship between the thermodynamic stabilities of variants of the model folding protein immunity protein 7 (Im7) fused into the resistance markers and their antibiotic resistance readouts. We also use this system to investigate the in vivo properties of the yeast prions Sup35 and Rnq1, and proteins whose aggregation is associated with some of the most prevalent neurodegenerative misfolding disorders, including peptide amyloid beta 1-42 (Aβ42), which is involved in Alzheimer’s disease, and protein synuclein, which is linked to Parkinson’s disease.
A Qualitative Analysis of Oncology Patient Awareness of Medication Shortages and Their Preferences for How Shortages Should Be Managed.
June 1, 2020
Clinicopathological and prognostic significance of circulating tumor cells in head and neck squamous cell carcinoma: A systematic review and meta-analysis.
March 18, 2020
Vaccine Effectiveness Against Influenza Hospitalization Among Children in the United States, 2015-2016.
March 2, 2020
July 17, 2019
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