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Issue 4, 2011
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Linking amyloid protein aggregation and yeast survival

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Abstract

Protein aggregation and amyloid formation lie behind an increasing number of human diseases. Here we describe the application of an “aggregation reporter”, in which the test protein is fused to dihydrofolate reductase, as a general method to assess the intracellular solubility of amyloid proteins in eukaryotic background. Because the aggregation state of the target protein is linked directly to yeast cells survival in the presence of methotrexate, protein solubility can be monitored in vivo without the requirement of a functional assay for the protein of interest. In addition, the approach allows the in vivo visualization of the cellular location and aggregated state of the target protein. To demonstrate the applicability of the assay in the screening of genes or compounds that modulate amyloid protein aggregation in living cells, we have used as models the Alzheimer's amyloid β peptide, polyglutamine expansions of huntingtin, α-synuclein and non-aggregating variants thereof. Moreover, the anti-aggregational properties of small molecules and the effects of the yeast protein quality control machinery have also been evaluated using this method.

Graphical abstract: Linking amyloid protein aggregation and yeast survival

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Publication details

The article was received on 23 Nov 2010, accepted on 19 Dec 2010 and first published on 14 Jan 2011


Article type: Paper
DOI: 10.1039/C0MB00297F
Citation: Mol. BioSyst., 2011,7, 1121-1128
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    Linking amyloid protein aggregation and yeast survival

    M. Morell, N. S. de Groot, J. Vendrell, F. X. Avilés and S. Ventura, Mol. BioSyst., 2011, 7, 1121
    DOI: 10.1039/C0MB00297F

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