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A fluorescence correlation spectroscopy study of ligand interaction with cytokinin-specific binding protein from mung bean

A fluorescence correlation spectroscopy study of ligand interaction with cytokinin-specific... Cytokinins are essential plant hormones that regulate numerous physiological processes. Recently, a protein was identified in mung bean ( Vigna radiata ) and characterized as a cytokinin-specific binding protein (VrCSBP). Fluorescence correlation spectroscopy was used to investigate the interaction between VrCSBP and its ligands. The synthetic cytokinin, N -phenyl- N ′-(4-pyridyl) urea, was labeled with two fluorophores, 7-nitro-2,1,3-benzoxadiazole and rhodamine B. Protein-ligand binding was analyzed in an equilibrium saturation binding experiment and confirmed by the competition assay. Surprisingly, it was found that VrCSBP binds not only to cytokinins, but also to gibberellins. In addition, in the presence of natural cytokinins and gibberellins, two populations of VrCSBP that differ in their diffusion coefficients were detected. The diffusion coefficients of these two populations could be related to mono- and dimeric states, which suggests a new mode of operation in ligand binding by VrCSBP, in which dimerization induced by natural ligands enhances the ligand binding capacity of the protein. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biological Chemistry de Gruyter

A fluorescence correlation spectroscopy study of ligand interaction with cytokinin-specific binding protein from mung bean

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References (30)

Publisher
de Gruyter
Copyright
©2010 by Walter de Gruyter Berlin New York
Subject
PROTEIN STRUCTURE AND FUNCTION
ISSN
1431-6730
eISSN
1437-4315
DOI
10.1515/BC.2010.005
pmid
19919180
Publisher site
See Article on Publisher Site

Abstract

Cytokinins are essential plant hormones that regulate numerous physiological processes. Recently, a protein was identified in mung bean ( Vigna radiata ) and characterized as a cytokinin-specific binding protein (VrCSBP). Fluorescence correlation spectroscopy was used to investigate the interaction between VrCSBP and its ligands. The synthetic cytokinin, N -phenyl- N ′-(4-pyridyl) urea, was labeled with two fluorophores, 7-nitro-2,1,3-benzoxadiazole and rhodamine B. Protein-ligand binding was analyzed in an equilibrium saturation binding experiment and confirmed by the competition assay. Surprisingly, it was found that VrCSBP binds not only to cytokinins, but also to gibberellins. In addition, in the presence of natural cytokinins and gibberellins, two populations of VrCSBP that differ in their diffusion coefficients were detected. The diffusion coefficients of these two populations could be related to mono- and dimeric states, which suggests a new mode of operation in ligand binding by VrCSBP, in which dimerization induced by natural ligands enhances the ligand binding capacity of the protein.

Journal

Biological Chemistryde Gruyter

Published: Jan 1, 2010

Keywords: cytokinin; gibberellins; phytohormone-binding protein; protein-ligand interactions; rhodamine B

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