Related Experiment Video
Updated: Aug 7, 2026

Detection of Protein Interactions in Plant using a Gateway Compatible Bimolecular Fluorescence Complementation (BiFC) System
Published on: September 16, 2011
Floral transcription factor AGAMOUS interacts in vitro with a leucine-rich repeat and an acid phosphatase protein
A Gamboa1, J Paéz-Valencia, G F Acevedo
1Laboratorio de Genética Molecular y Evolución, Instituto de Ecología, Universidad Nacional Autónoma de México, Ap. Postal 70-275, México DF, 04510, México.
Abstract:
We are interested in identifying potential protein interactors of MADS domain transcription factors during Arabidopsis thaliana flower development. We based our biochemical search on a conserved motif in the MADS domain that includes putative phosphatase and phosphorylation sites that may mediate protein interactions. An affinity column with this motif and a few surrounding hypervariable amino acids derived from the AGAMOUS sequence was prepared and used to isolate potential interactors from floral crude extracts. Only two proteins were specifically bound to the affinity column. The first corresponds to a carpel specific storage protein, VSP1, that presents acid phosphatase activity, and the second is a novel leucine-rich repeat protein that we have named FLOR1. Coimmunoprecipitation, two-hybrid yeast, and affinity column assays show that the FLOR1-VSP1 complex interacts with AGAMOUS and that this transcription factor directly interacts with FLOR1. This is the first assay to show an interaction between plant MADS domain factors and non-MADS proteins.
More Related Videos
12:36Chromatin Immunoprecipitation Assay for the Identification of Arabidopsis Protein-DNA Interactions In Vivo
Published on: January 14, 2016
11:33Investigating Interactions Between Histone Modifying Enzymes and Transcription Factors in vivo by Fluorescence Resonance Energy Transfer
Published on: October 14, 2022
Related Concept Videos
RNA Polymerase II Accessory Proteins
Cell Specific Gene Expression
Co-activators and Co-repressors
Eukaryotic Transcription Activators
The binding domains are capable of recognizing and interacting with regulatory sequences on the DNA. These domains are...
Eukaryotic Transcription Inhibitors
Eukaryotic transcription inhibitors usually contain two distinct domains, a DNA...
General Transcription Factors