|
Plant Physiol, June 2001, Vol. 126, pp. 601-612
The Mitochondrial Isovaleryl-Coenzyme A Dehydrogenase of
Arabidopsis Oxidizes Intermediates of Leucine and Valine
Catabolism1
Klaus
Däschner,
Ivan
Couée, and
Stefan
Binder*
Molekulare Botanik, Universität Ulm, Albert Einstein Allee
11, 89069 Ulm, Germany (K.D., S.B.); and Université de Rennes 1, Centre National de la Recherche Scientifique, Unité Mixte de
Recherche 6553 Fonctionnement des Ecosystèmes et Biologie de la
Conservation, 263 Avenue du Général Leclerc, CS
74205, 35042 Rennes cedex, France (I.C.)
We recently identified a cDNA encoding a putative
isovaleryl-coenzyme A (CoA) dehydrogenase in Arabidopsis
(AtIVD). In animals, this homotetrameric enzyme is located in
mitochondria and catalyzes the conversion of isovaleryl-CoA to
3-methylcrotonyl-CoA as an intermediate step in the leucine (Leu)
catabolic pathway. Expression of AtIVD:smGFP4 fusion proteins in
tobacco (Nicotiana tabacum) protoplasts and
biochemical studies now demonstrate the in vivo import of the plant
isovaleryl-CoA dehydrogenase (IVD) into mitochondria and the enzyme in
the matrix of these organelles. Two-dimensional separation of
mitochondrial proteins by blue native and SDS-PAGE and size
determination of the native and overexpressed proteins suggest
homodimers to be the dominant form of the plant IVD. Northern-blot hybridization and studies in transgenic Arabidopsis plants expressing Ativd promoter:gus constructs reveal strong expression of this gene in
seedlings and young plants grown in the absence of sucrose, whereas
promoter activity in almost all tissues is strongly inhibited by
exogeneously added sucrose. Substrate specificity tests with AtIVD
expressed in Escherichia coli indicate a strong
preference toward isovaleryl-CoA but surprisingly also show
considerable activity with isobutyryl-CoA. This strongly indicates a
commitment of the enzyme in Leu catabolism, but the activity observed
with isobutyryl-CoA also suggests a parallel involvement of the enzyme in the dehydrogenation of intermediates of the valine degradation pathway. Such a dual activity has not been observed with the animal IVD
and may suggest a novel connection of the Leu and valine catabolism in
plants.
1
This work was supported by the Fonds der
Chemischen Industrie and by the Anfangsförderung der
Universität Ulm.
*
Corresponding author; e-mail stefan.binder{at}biologie.uni-ulm.de;
fax 49-731-50-22626.
© 2001 American Society of Plant Physiologists
This article has been cited by other articles:
|
|
|
|
 
W. G. van Doorn and E. J. Woltering
Physiology and molecular biology of petal senescence
J. Exp. Bot.,
March 3, 2008;
(2008)
erm356v2.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
K. Forster-Fromme, A. Chattopadhyay, and D. Jendrossek
Biochemical characterization of AtuD from Pseudomonas aeruginosa, the first member of a new subgroup of acyl-CoA dehydrogenases with specificity for citronellyl-CoA
Microbiology,
March 1, 2008;
154(3):
789 - 796.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
A. Matthes, S. Schmidt-Gattung, D. Kohler, J. Forner, S. Wildum, M. Raabe, H. Urlaub, and S. Binder
Two DEAD-Box Proteins May Be Part of RNA-Dependent High-Molecular-Mass Protein Complexes in Arabidopsis Mitochondria
Plant Physiology,
December 1, 2007;
145(4):
1637 - 1646.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
K. A. Lucas, J. R. Filley, J. M. Erb, E. R. Graybill, and J. W. Hawes
Peroxisomal Metabolism of Propionic Acid and Isobutyric Acid in Plants
J. Biol. Chem.,
August 24, 2007;
282(34):
24980 - 24989.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
J. Schuster, T. Knill, M. Reichelt, J. Gershenzon, and S. Binder
BRANCHED-CHAIN AMINOTRANSFERASE4 Is Part of the Chain Elongation Pathway in the Biosynthesis of Methionine-Derived Glucosinolates in Arabidopsis
PLANT CELL,
October 1, 2006;
18(10):
2664 - 2679.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
K. Ishizaki, T. R. Larson, N. Schauer, A. R. Fernie, I. A. Graham, and C. J. Leaver
The Critical Role of Arabidopsis Electron-Transfer Flavoprotein:Ubiquinone Oxidoreductase during Dark-Induced Starvation
PLANT CELL,
September 1, 2005;
17(9):
2587 - 2600.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
E. S. Goetzman, A.-W. A. Mohsen, K. Prasad, and J. Vockley
Convergent Evolution of a 2-Methylbutyryl-CoA Dehydrogenase from Isovaleryl-CoA Dehydrogenase in Solanum tuberosum
J. Biol. Chem.,
February 11, 2005;
280(6):
4873 - 4879.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
N. L. Taylor, J. L. Heazlewood, D. A. Day, and A. H. Millar
Lipoic Acid-Dependent Oxidative Catabolism of {alpha}-Keto Acids in Mitochondria Provides Evidence for Branched-Chain Amino Acid Catabolism in Arabidopsis
Plant Physiology,
February 1, 2004;
134(2):
838 - 848.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
R. Diebold, J. Schuster, K. Daschner, and S. Binder
The Branched-Chain Amino Acid Transaminase Gene Family in Arabidopsis Encodes Plastid and Mitochondrial Proteins
Plant Physiology,
June 1, 2002;
129(2):
540 - 550.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
P. Che, E. S. Wurtele, and B. J. Nikolau
Metabolic and Environmental Regulation of 3-Methylcrotonyl-Coenzyme A Carboxylase Expression in Arabidopsis
Plant Physiology,
June 1, 2002;
129(2):
625 - 637.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
