|
Originally published In Press as doi:10.1074/jbc.M302154200 on April 24, 2003
J. Biol. Chem., Vol. 278, Issue 27, 24966-24975, July 4, 2003
The Plant Biotin Synthase Reaction
IDENTIFICATION AND CHARACTERIZATION OF ESSENTIAL MITOCHONDRIAL ACCESSORY PROTEIN COMPONENTS*
Antoine Picciocchi ,
Roland Douce and
Claude Alban ¶
From the
Laboratoire Mixte de Recherche, CNRS/Institut National de la Recherche Agronomique (INRA)/Bayer CropScience (UMR 1932), Bayer CropScience, 14-20 Rue Pierre Baizet, 69263 Lyon Cedex 9, France
In plants, the last step of the biotin biosynthetic pathway is localized in mitochondria. This chemically complex reaction is catalyzed by the biotin synthase protein, encoded by the bio2 gene in Arabidopsis thaliana. Unidentified mitochondrial proteins in addition to the bio2 gene product are obligatory for the reaction to occur. In order to identify these additional proteins, potato mitochondrial matrix was fractionated onto different successive chromatographic columns. Combination experiments using purified Bio2 protein and the resulting mitochondrial matrix subfractions together with a genomic based research allowed us to identify mitochondrial adrenodoxin, adrenodoxin reductase, and cysteine desulfurase (Nfs1) proteins as essential components for the plant biotin synthase reaction. Arabidopsis cDNAs encoding these proteins were cloned, and the corresponding proteins were expressed in Escherichia coli cells and purified. Purified recombinant adrenodoxin and adrenodoxin reductase proteins formed in vitro an efficient low potential electron transfer chain that interacted with the bio2 gene product to reconstitute a functional plant biotin synthase complex. Bio2 from Arabidopsis is the first identified protein partner for this specific plant mitochondrial redox chain.
Received for publication, March 3, 2003
, and in revised form, April 10, 2003.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AY074925, AY074926, AY074927, and AF229854.
* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
Present address: UMR 5019 CNRS/Commissariat à l'Energie Atomique (CEA)/Université Joseph Fourier/INRA, CEA-Grenoble, Dépt. Réponse et Dynamique Cellulaires, Laboratoire de Physiologie Cellulaire Végétale, 17 rue des Martyrs, 38054 Grenoble Cedex 9, France.
Present address: Institut de Biologie Structurale, 41, rue Jules Horowitz, 38027 Grenoble Cedex 1, France.
¶ To whom correspondence should be addressed: UMR 5019 CNRS/Commissariat à l'Energie Atomique (CEA)/Université Joseph Fourier/INRA, CEA-Grenoble, Dépt. Réponse et Dynamique Cellulaires, Laboratoire de Physiologie Cellulaire Végétale, 17 rue des Martyrs, 38054 Grenoble Cedex 9, France. Tel.: 33-438-78-23-63; Fax: 33-438-78-50-91; E-mail: calban{at}cea.fr.

CiteULike Complore Connotea Del.icio.us Digg Reddit Technorati What's this?
This article has been cited by other articles:

|
 |

|
 |
 
A. Atteia, A. Adrait, S. Brugiere, M. Tardif, R. van Lis, O. Deusch, T. Dagan, L. Kuhn, B. Gontero, W. Martin, et al.
A Proteomic Survey of Chlamydomonas reinhardtii Mitochondria Sheds New Light on the Metabolic Plasticity of the Organelle and on the Nature of the {alpha}-Proteobacterial Mitochondrial Ancestor
Mol. Biol. Evol.,
July 1, 2009;
26(7):
1533 - 1548.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
S. Huang, N. L. Taylor, R. Narsai, H. Eubel, J. Whelan, and A. H. Millar
Experimental Analysis of the Rice Mitochondrial Proteome, Its Biogenesis, and Heterogeneity
Plant Physiology,
February 1, 2009;
149(2):
719 - 734.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
F. H. Haas, C. Heeg, R. Queiroz, A. Bauer, M. Wirtz, and R. Hell
Mitochondrial Serine Acetyltransferase Functions as a Pacemaker of Cysteine Synthesis in Plant Cells
Plant Physiology,
October 1, 2008;
148(2):
1055 - 1067.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
J. Godman and J. Balk
Genome Analysis of Chlamydomonas reinhardtii Reveals The Existence of Multiple, Compartmentalized Iron-Sulfur Protein Assembly Machineries of Different Evolutionary Origins
Genetics,
May 1, 2008;
179(1):
59 - 68.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
R. Muralla, E. Chen, C. Sweeney, J. A. Gray, A. Dickerman, B. J. Nikolau, and D. Meinke
A Bifunctional Locus (BIO3-BIO1) Required for Biotin Biosynthesis in Arabidopsis
Plant Physiology,
January 1, 2008;
146(1):
60 - 73.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
L. Palmieri, R. Arrigoni, E. Blanco, F. Carrari, M. I. Zanor, C. Studart-Guimaraes, A. R. Fernie, and F. Palmieri
Molecular Identification of an Arabidopsis S-Adenosylmethionine Transporter. Analysis of Organ Distribution, Bacterial Expression, Reconstitution into Liposomes, and Functional Characterization
Plant Physiology,
November 1, 2006;
142(3):
855 - 865.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
O. Onder, H. Yoon, B. Naumann, M. Hippler, A. Dancis, and F. Daldal
Modifications of the Lipoamide-containing Mitochondrial Subproteome in a Yeast Mutant Defective in Cysteine Desulfurase
Mol. Cell. Proteomics,
August 1, 2006;
5(8):
1426 - 1436.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
V. Pinon, S. Ravanel, R. Douce, and C. Alban
Biotin Synthesis in Plants. The First Committed Step of the Pathway Is Catalyzed by a Cytosolic 7-Keto-8-Aminopelargonic Acid Synthase
Plant Physiology,
December 1, 2005;
139(4):
1666 - 1676.
[Abstract]
[Full Text]
[PDF]
|
 |
|
Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.
|
Advertisement
Advertisement
|