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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2017: 3.022

CiteScore 2017: 2.81

SCImago Journal Rank (SJR) 2017: 1.562
Source Normalized Impact per Paper (SNIP) 2017: 0.705

Online
ISSN
1437-4315
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Volume 391, Issue 1

Issues

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

Paweł Zawadzki
  • Department of Molecular and Cellular Biology, Faculty of Biology, Adam Mickiewicz University, Umultowska 89, 61-614 Poznań, Poland
  • Department of Molecular Biophysics, Faculty of Physics, Adam Mickiewicz University, Umultowska 85, 61-614 Poznań, Poland
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Genowefa Ślósarek
  • Department of Molecular Biophysics, Faculty of Physics, Adam Mickiewicz University, Umultowska 85, 61-614 Poznań, Poland
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Jerzy Boryski
  • Institute of Bioorganic Chemistry, Polish Academy of Sciences, Noskowskiego 12/14, 61-704 Poznań, Poland
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Przemysław Wojtaszek
  • Department of Molecular and Cellular Biology, Faculty of Biology, Adam Mickiewicz University, Umultowska 89, 61-614 Poznań, Poland
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2009-11-17 | DOI: https://doi.org/10.1515/bc.2010.005

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.

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

About the article

Corresponding author


Received: 2009-08-21

Accepted: 2009-09-16

Published Online: 2009-11-17

Published in Print: 2010-01-01


Citation Information: Biological Chemistry, Volume 391, Issue 1, Pages 43–53, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/bc.2010.005.

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