ArticleMethods in molecular biology (Clifton, N.J.)2026
Deciphering Protein Interaction Dynamics Using the Yeast Three-Hybrid System.
Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Proteins often act together with other proteins to regulate crucial biological processes. Beyond binary interactions, they often operate within multi-protein assemblies, where alterations in binding affinity or structural conformation of one or more components can significantly impact the overall function of the complex. The yeast three-hybrid (Y3H) system extends the conventional yeast two-hybrid (Y2H) by adding a bridge protein to test ternary interactions ex planta. Here, we present a Y3H protocol utilizing the pBridge and pACT2 AD vectors in the Saccharomyces cerevisiae Y2HGold strain and examine the role of SUPPRESSOR OF PHYA-105 1 (SPA1) in mediating the interaction between CONSTITUTIVE PHOTOMORPHOGENIC 1 (COP1) and CRYPTOCHROME 1 (CRY1) in Arabidopsis thaliana. COP1 and SPA proteins form a functional E3 ubiquitin ligase complex that prevents photomorphogenesis in darkness, while CRY1 antagonizes this activity under blue light conditions. Using the Y3H system, we show that co-expression of SPA1 enhances the interaction between COP1 and CRY1, as detected via MEL1 reporter gene activation in a quantitative assay using p-nitrophenyl alpha-D-galactopyranoside (PNPG). This protocol offers a practical framework for dissecting ternary protein interactions using the Y3H assay.
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