Improving analytical methods for protein-protein interaction through implementation of chemically inducible dimerization.

ABSTRACT: When investigating interactions between two proteins with complementary reporter tags in yeast two-hybrid or split GFP assays, it remains troublesome to discriminate true- from false-negative results and challenging to compare the level of interaction across experiments. This leads to decreased sensitivity and renders analysis of weak or transient interactions difficult to perform. In this work, we describe the development of reporters that can be chemically induced to dimerize independently of the investigated interactions and thus alleviate these issues. We incorporated our reporters into the widely used split ubiquitin-, bimolecular fluorescence complementation (BiFC)- and Förster resonance energy transfer (FRET)- based methods and investigated different protein-protein interactions in

SUBMITTER: Andersen TG 

PROVIDER: S-EPMC4901268 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature