Microscale Thermophoresis (MST) to Study Rapid Alkalinization Factor (RALF)-Receptor Interactions

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Serval ID
serval:BIB_E5AFC000D9D7
Type
A part of a book
Publication sub-type
Chapter: chapter ou part
Collection
Publications
Institution
Title
Microscale Thermophoresis (MST) to Study Rapid Alkalinization Factor (RALF)-Receptor Interactions
Title of the book
Plant Peptide Hormones and Growth Factors
Author(s)
Gonneau Martine, Schoenaers Sébastjen, Broyart Caroline, Vissenberg Kris, Santiago Julia, Höfte Herman
Publisher
Springer US
ISBN
9781071635100
9781071635117
ISSN
1064-3745
1940-6029
ISSN-L
1064-3745
Publication state
Published
Issued date
2024
Peer-reviewed
Oui
Volume
2731
Series
Methods in Molecular Biology
Pages
279-293
Language
english
Abstract
Microscale thermophoresis (MST) is a simple but powerful tool to study the in vitro interaction among biomolecules, and to quantify binding affinities. MST curves describe the change in the fluorescence level of a fluorescent target as a result of an IR-laser-induced temperature change. The degree and nature of the change in fluorescence signal depends on the size, charge, and solvation shell of the molecules, properties that change in function of the binding of a ligand to the fluorescent target.We used MST to describe the interaction between components of a regulatory module involved in plant cell wall integrity control. This module comprises the secreted peptide Rapid Alkalinization Factor 23 (RALF23) and its receptor complex consisting of the GPI-anchored receptor Lorelei-Like Glycoprotein 1 (LLG1) and a receptor kinase of the CrRLK1L family, FERONIA. Here we show how MST can also be used to study three-partner interactions.
Keywords
Biological Transport, Cell Membrane, Cell Wall, Coloring Agents, Fluorescence, Binding affinity, Feronia (FER), Lorelei Like Glycoprotein (LLG), Molecular interaction, Rapid Alkalinization Factor (RALF), Receptor complex formation, Soret effect, Thermophoresis
Pubmed
Create date
04/12/2023 14:33
Last modification date
12/04/2024 7:45
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