Rewiring the budding yeast proteome using synthetic physical interactions
Authors list
Guðjón Ólafsson Peter H ThorpeAbstract
Artificially tethering two proteins or protein fragments together is a powerful method to query molecular mechanisms. However, this approach typically relies upon a prior understanding of which two proteins, when fused, are most likely to provide a specific function and is therefore not readily amenable to large-scale screening. Here, we describe the Synthetic Physical Interaction (SPI) method to create proteome-wide forced protein associations in the budding yeast Saccharomyces cerevisiae. This method allows thousands of protein-protein associations to be screened for those that affect either normal growth or sensitivity to drugs or specific conditions. The method is amenable to proteins, protein domains, or any genetically encoded peptide sequence.
Journal details
Journal Methods in Molecular Biology
Volume 1672
Pages 599-612
Available online
Publication date
Full text links
Publisher website (DOI) 10.1007/978-1-4939-7306-4_39
Europe PubMed Central 29043650
Pubmed 29043650
Keywords
Related topics
Type of publication