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- Title
Isolation and characterization of aD-cysteine desulfhydrase protein fromArabidopsis thaliana.
- Authors
Riemenschneider, Anja; Wegele, Rosalina; Schmidt, Ahlert; Papenbrock, Jutta
- Abstract
In several organismsd-cysteine desulfhydrase (d-CDes) activity (EC 4.1.99.4) was measured; this enzyme decomposesd-cysteine into pyruvate, H2S, and NH3. A gene encoding a putatived-CDes protein was identified inArabidopsis thaliana(L) Heynh. based on high homology to anEscherichia coliprotein called YedO that hasd-CDes activity. The deducedArabidopsisprotein consists of 401 amino acids and has a molecular mass of 43.9 kDa. It contains a pyridoxal-5′-phosphate binding site. The purified recombinant mature protein had aKm ford-cysteine of 0.25 mm. Onlyd-cysteine but notl-cysteine was converted byd-CDes to pyruvate, H2S, and NH3. The activity was inhibited by aminooxy acetic acid and hydroxylamine, inhibitors specific for pyridoxal-5′-phosphate dependent proteins, at low micromolar concentrations. The protein did not exhibit 1-aminocyclopropane-1-carboxylate deaminase activity (EC 3.5.99.7) as homologous bacterial proteins. Western blot analysis of isolated organelles and localization studies using fusion constructs with the green fluorescent protein indicated an intracellular localization of the nuclear encodedd-CDes protein in the mitochondria.d-CDes RNA levels increased with proceeding development ofArabidopsisbut decreased in senescent plants;d-CDes protein levels remained almost unchanged in the same plants whereas specificd-CDes activity was highest in senescent plants. In plants grown in a 12-h light/12-h dark rhythmd-CDes RNA levels were highest in the dark, whereas protein levels and enzyme activity were lower in the dark period than in the light indicating post-translational regulation. Plants grown under low sulfate concentration showed an accumulation ofd-CDes RNA and increased protein levels, thed-CDes activity was almost unchanged. Putativein vivofunctions of theArabidopsisd-CDes protein are discussed.
- Subjects
CYSTATHIONINE gamma-lyase; ARABIDOPSIS thaliana; ARABIDOPSIS; PROTEINS; AMINO acids; GENES
- Publication
FEBS Journal, 2005, Vol 272, Issue 5, p1291
- ISSN
1742-464X
- Publication type
Article
- DOI
10.1111/j.1742-4658.2005.04567.x