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| Home > Publications database > Accurate and sensitive interactome profiling using a quantitative protein-fragment complementation assay. |
| Journal Article | DKFZ-2024-02167 |
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2024
Cell Press
Cambridge, MA
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Please use a persistent id in citations: doi:10.1016/j.crmeth.2024.100880
Abstract: An accurate description of protein-protein interaction (PPI) networks is key to understanding the molecular mechanisms underlying cellular systems. Here, we constructed genome-wide libraries of yeast strains to systematically probe protein-protein interactions using NanoLuc Binary Technology (NanoBiT), a quantitative protein-fragment complementation assay (PCA) based on the NanoLuc luciferase. By investigating an array of well-documented PPIs as well as the interactome of four proteins with varying levels of characterization-including the well-studied nonsense-mediated mRNA decay (NMD) regulator Upf1 and the SCF complex subunits Cdc53 and Met30-we demonstrate that ratiometric NanoBiT measurements enable highly precise and sensitive mapping of PPIs. This work provides a foundation for employing NanoBiT in the assembly of more comprehensive and accurate protein interaction maps as well as in their functional investigation.
Keyword(s): Protein Interaction Mapping: methods (MeSH) ; Saccharomyces cerevisiae: genetics (MeSH) ; Saccharomyces cerevisiae: metabolism (MeSH) ; Protein Interaction Maps (MeSH) ; Saccharomyces cerevisiae Proteins: metabolism (MeSH) ; Saccharomyces cerevisiae Proteins: genetics (MeSH) ; Luciferases: genetics (MeSH) ; Luciferases: metabolism (MeSH) ; CP: Systems biology ; Cdc53 ; Irc20 ; Met30 ; Nam7 ; NanoBiT ; Saccharomyces cerevisiae ; Upf1 ; budding yeast ; interactome ; protein-protein interaction ; Saccharomyces cerevisiae Proteins ; Luciferases
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