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Title: Engineering functional artificial hybrid proteins between poplar peroxiredoxin II and glutaredoxin or thioredoxin

Abstract

The existence of natural peroxiredoxin-glutaredoxin hybrid enzymes in several bacteria is in line with previous findings indicating that poplar peroxiredoxin II can use glutaredoxin as an electron donor. This peroxiredoxin remains however unique since it also uses thioredoxin with a quite good efficiency. Based on the existing fusions, we have created artificial enzymes containing a poplar peroxiredoxin module linked to glutaredoxin or thioredoxin modules. The recombinant fusion enzymes folded properly into non-covalently bound homodimers or homotetramers. Two of the three protein constructs exhibit peroxidase activity, a reaction where the two modules need to function together, but they also display enzymatic activities specific of each module. In addition, mass spectrometry analyses indicate that the Prx module can be both glutathiolated or overoxidized in vitro. This is discussed in the light of the Prx reactivity.

Authors:
 [1];  [2];  [3];  [2];  [4];  [2]
  1. UMR 1136 Interactions Arbres Microorganismes INRA UHP, IFR 110 GEEF, Faculte des Sciences, BP 239 54506 Vandoeuvre-les-Nancy Cedex (France). E-mail: nrouhier@scbiol.uhp-nancy.fr
  2. UMR 1136 Interactions Arbres Microorganismes INRA UHP, IFR 110 GEEF, Faculte des Sciences, BP 239 54506 Vandoeuvre-les-Nancy Cedex (France)
  3. Umea Plant Science Centre, Swedish University of Agricultural Sciences, Department of Forest Genetics and Plant Physiology, SE-901 83 Umea (Sweden)
  4. Laboratoire de Resonance Magnetique Nucleaire, Institut de Biologie Structurale CEA-CNRS-UJF 'Jean-Pierre Ebel' 41 Avenue Jules Horowitz, 38027 Grenoble Cedex 1 (France)
Publication Date:
OSTI Identifier:
20798860
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 341; Journal Issue: 4; Other Information: DOI: 10.1016/j.bbrc.2006.01.099; PII: S0006-291X(06)00192-6; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; BACTERIA; BINDING ENERGY; HYBRIDIZATION; IN VITRO; MASS SPECTROSCOPY; PEROXIDASES; POPLARS; REACTIVITY

Citation Formats

Rouhier, Nicolas, Gama, Filipe, Wingsle, Gunnar, Gelhaye, Eric, Gans, Pierre, and Jacquot, Jean-Pierre. Engineering functional artificial hybrid proteins between poplar peroxiredoxin II and glutaredoxin or thioredoxin. United States: N. p., 2006. Web. doi:10.1016/j.bbrc.2006.01.099.
Rouhier, Nicolas, Gama, Filipe, Wingsle, Gunnar, Gelhaye, Eric, Gans, Pierre, & Jacquot, Jean-Pierre. Engineering functional artificial hybrid proteins between poplar peroxiredoxin II and glutaredoxin or thioredoxin. United States. doi:10.1016/j.bbrc.2006.01.099.
Rouhier, Nicolas, Gama, Filipe, Wingsle, Gunnar, Gelhaye, Eric, Gans, Pierre, and Jacquot, Jean-Pierre. Fri . "Engineering functional artificial hybrid proteins between poplar peroxiredoxin II and glutaredoxin or thioredoxin". United States. doi:10.1016/j.bbrc.2006.01.099.
@article{osti_20798860,
title = {Engineering functional artificial hybrid proteins between poplar peroxiredoxin II and glutaredoxin or thioredoxin},
author = {Rouhier, Nicolas and Gama, Filipe and Wingsle, Gunnar and Gelhaye, Eric and Gans, Pierre and Jacquot, Jean-Pierre},
abstractNote = {The existence of natural peroxiredoxin-glutaredoxin hybrid enzymes in several bacteria is in line with previous findings indicating that poplar peroxiredoxin II can use glutaredoxin as an electron donor. This peroxiredoxin remains however unique since it also uses thioredoxin with a quite good efficiency. Based on the existing fusions, we have created artificial enzymes containing a poplar peroxiredoxin module linked to glutaredoxin or thioredoxin modules. The recombinant fusion enzymes folded properly into non-covalently bound homodimers or homotetramers. Two of the three protein constructs exhibit peroxidase activity, a reaction where the two modules need to function together, but they also display enzymatic activities specific of each module. In addition, mass spectrometry analyses indicate that the Prx module can be both glutathiolated or overoxidized in vitro. This is discussed in the light of the Prx reactivity.},
doi = {10.1016/j.bbrc.2006.01.099},
journal = {Biochemical and Biophysical Research Communications},
number = 4,
volume = 341,
place = {United States},
year = {Fri Mar 24 00:00:00 EST 2006},
month = {Fri Mar 24 00:00:00 EST 2006}
}