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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

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

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1437-4315
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Volume 386, Issue 11 (Nov 2005)

Issues

Monitoring the real-time kinetics of the hydrolysis reaction of guanine nucleotide-binding proteins

Alexander Eberth
  • Department of Structural Biology, Max-Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, D-44227 Dortmund, Germany
/ Radovan Dvorsky
  • Department of Structural Biology, Max-Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, D-44227 Dortmund, Germany
/ Christian F.W. Becker
  • Department of Physical Biochemistry, Max-Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, D-44227 Dortmund, Germany
/ Andrea Beste
  • Department of Physical Biochemistry, Max-Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, D-44227 Dortmund, Germany
/ Roger S. Goody
  • Department of Physical Biochemistry, Max-Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, D-44227 Dortmund, Germany and Institute of Physiological Chemistry, Ruhr University, D-44801 Bochum, Germany
/ Mohammad Reza Ahmadian
  • Department of Structural Biology, Max-Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, D-44227 Dortmund, Germany
Published Online: 2005-11-24 | DOI: https://doi.org/10.1515/BC.2005.127

Abstract

The conversion of guanosine triphosphate (GTP) to guanosine diphosphate (GDP) and inorganic phosphate (Pi) by guanine nucleotide-binding proteins (GNBPs) is a fundamental enzyme reaction in living cells that acts as an important timer in a variety of biological processes. This reaction is intrinsically slow but can be stimulated by GTPase-activating proteins (GAPs) by several orders of magnitude. In the present study, we synthesized and characterized a new fluorescent nucleotide, 2′(3′)-O-(N-ethylcarbamoyl-(5″-carboxytetramethylrhodamine) amide)-GTP, or tamraGTP, which is sensitive towards conformational changes of certain GNBPs induced by GTP hydrolysis. Unlike other fluorescent nucleotides, tamra-GTP allows real-time monitoring of the kinetics of the intrinsic and GAP-catalyzed GTP hydrolysis reactions of small GNBPs from the Rho family.

Keywords: fluorescence reporter; GTPase; GTPase-activating protein; GTP hydrolysis; guanine nucleotide-binding protein; rhodamine; spectroscopy

About the article

Corresponding author


Received: July 7, 2005

Accepted: August 30, 2005

Published Online: 2005-11-24

Published in Print: 2005-11-01


Citation Information: Biological Chemistry, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2005.127.

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