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Related Experiment Video

Updated: Jan 29, 2026

Pull-down of Calmodulin-binding Proteins

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

Optimized small-molecule pull-downs define MLBP1 as an acyl-lipid-binding protein.

Yelena Sterlin¹, Oded Pri-Tal¹, Gil Zimran¹

¹The Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, the Hebrew University of Jerusalem, Rehovot, 7610001, Israel.

The Plant Journal : for Cell and Molecular Biology

|February 9, 2019

Summary

This summary is machine-generated.

Researchers identified new plant hormone ligands using a novel affinity purification method. This technique successfully uncovered monolinolenin binding to the MLBP1 protein in Arabidopsis, advancing our understanding of plant signaling pathways.

Keywords:

PYR/PYL/RCAR in planta ABA signaling Bet v 1 START domain abscisic acid polyketide cyclase-like proteins protein-metabolite interactions technical advance

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Area of Science:

Plant Biology
Biochemistry
Molecular Biology

Background:

Abscisic acid (ABA) receptors are START domain proteins crucial for plant signaling.
While ABA receptors are well-studied, many other START domain proteins lack identified ligands.
Understanding these protein-ligand interactions is key to deciphering plant physiology.

Purpose of the Study:

To develop and optimize a method for identifying ligands of START domain proteins.
To discover novel protein-metabolite interactions within the START domain superfamily.
To investigate the ligand-binding capabilities of uncharacterized START domain proteins in plants.

Main Methods:

Utilized affinity purification of biotinylated proteins in Nicotiana benthamiana.
Employed untargeted liquid chromatography-mass spectrometry (LC-MS) for ligand identification.
Validated interactions using recombinant proteins and native extracts from transgenic Arabidopsis.

Main Results:

Optimized method confirmed known ABA-PYL interactions, demonstrating high sensitivity.
Identified monolinolenin as a ligand for MLBP1 (At4G01883).
Confirmed monolinolenin-MLBP1 interaction in both heterologous expression systems and native Arabidopsis context.

Conclusions:

The developed affinity purification-LC-MS method is effective for discovering plant protein-ligand interactions.
Monolinolenin is a novel ligand for the START domain protein MLBP1.
This study expands the known repertoire of plant START domain protein functions and their associated metabolites.