Identification of a major soluble protein in mitochondria from nonphotosynthetic tissues as NAD-dependent formate dehydrogenase
| Autor: | Françoise Ambard-Bretteville, René Rémy, C. C. des Francs-Small, Ian Small |
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| Přispěvatelé: | ProdInra, Migration, Unité de recherche Génétique et amélioration des plantes (GAP), Institut National de la Recherche Agronomique (INRA) |
| Jazyk: | angličtina |
| Rok vydání: | 1993 |
| Předmět: |
Physiology
Molecular Sequence Data Plant Science SEQUENCE PROTEIQUE Biology Formate dehydrogenase [SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics Pseudomonas Complementary DNA [SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants genetics Gene expression Genetics Amino Acid Sequence Cloning Molecular Photosynthesis Peptide sequence Polyacrylamide gel electrophoresis Gene Library Solanum tuberosum chemistry.chemical_classification Base Sequence Sequence Homology Amino Acid Nucleic acid sequence food and beverages NAD Formate Dehydrogenases Molecular biology Mitochondria Open reading frame Enzyme chemistry Biochemistry Research Article |
| Zdroj: | Scopus-Elsevier Plant Physiology Plant Physiology, American Society of Plant Biologists, 1993, 102, pp.1171-1177 |
| ISSN: | 0032-0889 1532-2548 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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