Significant reduction of BiFC non-specific assembly facilitates in planta assessment of heterotrimeric G-protein interactors.

ABSTRACT: Protein networks and signaling cascades are key mechanisms for intra- and intercellular signal transduction. Identifying the interacting partners of a protein can provide vital clues regarding its physiological role. The bimolecular fluorescence complementation (BiFC) assay has become a routine tool for in vivo analysis of protein-protein interactions and their subcellular location. Although the BiFC system has improved since its inception, the available options for in planta analysis are still subject to very low signal-to-noise ratios, and a systematic comparison of BiFC confounding background signals has been lacking. Background signals can obscure weak interactions, provide false positives, and decrease confidence in true positives. To overcome these problems, we performed an extensive

SUBMITTER: Gookin TE 

PROVIDER: S-EPMC4260091 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature