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PLANT PHYSIOLOGY , Vol 102, Issue 4 1171-1177, Copyright © 1993 by American Society of Plant Biologists
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MOLECULAR BIOLOGY AND GENE REGULATION |
Identification of a Major Soluble Protein in Mitochondria from Nonphotosynthetic Tissues as NAD-Dependent Formate Dehydrogenase
C. C. des Francs-Small, F. Ambard-Bretteville, I. D. Small and R. Remy
Laboratoire de Genetique Moleculaire des Plantes, Centre National de la Recherche Scientifique-Unite de Recherche Associee 1128, Universite Paris-Sud, Batiment 360, F-91405 Orsay Cedex, France (C.C.d.F.-S., F.A.-B., R.R.)
In many plant species, one of the most abundant soluble proteins (as judged
by two-dimensional polyacrylamide gel electrophoresis) in mitochondria from
nongreen tissues is a 40-kD polypeptide that is relatively scarce in
mitochondria from photosynthetic tissues. cDNA sequences encoding this
polypeptide were isolated from a [lambda]gt11 cDNA expression library from
potato (Solanum tuberosum L.) by screening with a specific antibody raised
against the 40-kD polypeptide. The cDNA sequence contains an open reading
frame of 1137 nucleotides whose predicted amino acid sequence shows strong
homology to an NAD-dependent formate dehydrogenase (EC 1.2.1.2) from
Pseudomonas sp. 101. Comparison of the cDNA sequence with the N-terminal
amino acid sequence of the mature 40-kD polypeptide suggests that the
polypeptide is made as a precursor with a 23-amino acid presequence that
shows characteristics typical of mitochondrial targeting signals. The
identity of the polypeptide was confirmed by assaying the formate
dehydrogenase activity in plant mitochondria from various tissues and by
activity staining of mitochondrial proteins run on native gels combined
with antibody recognition. The abundance and distribution of this protein
suggest that higher plant mitochondria from various non-photosynthetic
plant tissues (tubers, storage roots, seeds, dark-grown shoots, cauliflower
heads, and tissues grown in vitro) might contain a formate-producing
fermentation pathway similar to those described in bacteria and algae.
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