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Polyglutamine toxicity in yeast uncovers phenotypic variations between different fluorescent protein fusions
Author(s) -
Jiang Yuwei,
Di Gregorio Sonja E.,
Duennwald Martin L.,
Lajoie Patrick
Publication year - 2017
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/tra.12453
Subject(s) - biology , yeast , saccharomyces cerevisiae , toxicity , fusion protein , green fluorescent protein , fluorescence , phenotype , computational biology , microbiology and biotechnology , fusion , genetics , biochemistry , gene , recombinant dna , chemistry , physics , organic chemistry , quantum mechanics , linguistics , philosophy
The palette of fluorescent proteins ( FPs ) available for live‐cell imaging contains proteins that strongly differ in their biophysical properties. FPs cannot be assumed to be equivalent and in certain cases could significantly perturb the behavior of fluorescent reporters. We employed Saccharomyces cerevisiae to comprehensively study the impact of FPs on the toxicity of polyglutamine ( polyQ ) expansion proteins associated with Huntington's disease. The toxicity of polyQ fusion constructs is highly dependent on the sequences flanking the polyQ repeats. Thus, they represent a powerful tool to study the impact of fluorescent fusion partners. We observed significant differences on polyQ aggregation and toxicity between commonly used FPs . We generated a novel series of vectors with latest yeast‐optimized FPs for investigation of Htt toxicity, including a newly optimized blue FP for expression in yeast. Our study highlights the importance of carefully choosing the optimal FPs when designing tagging strategies.