Details
| Original language | English |
|---|---|
| Pages (from-to) | 861-870 |
| Number of pages | 10 |
| Journal | Plant physiology and biochemistry |
| Volume | 39 |
| Issue number | 10 |
| Publication status | Published - 1 Jan 2001 |
Abstract
The last step in cysteine biosynthesis is catalysed by the pyridoxal 5′-phosphate-dependent enzyme O-acetyl-L-serine(thiol)lyase (OAS-TL). Several isoforms are localized in different compartments of the cell. OAS-TL and OAS-TL-like proteins also catalyse the formation of β-cyanoalanine and sulfide; the release of sulfide and of an unknown product was also observed. In Arabidopsis plants of different age, the OAS-TL activity decreased with increasing age whereas the enzymatical sulfide release from cysteine increased in older plants. The β-cyanoalanine synthase showed two activity peaks during the time course investigated. During a 12-h light/12-h dark rhythm, the OAS-TL and the sulfide-releasing activities ran parallel with a maximum in the light phase and a decrease of enzyme activity in the dark phase. β-Cyanoalanine synthase activities did not follow a special pattern. Three genes coding for the OAS-TL isoforms A, B, and C, which are presumably localized in the cytoplasm, in plastids, and in mitochondria, respectively, were differentially expressed. The mRNA steady-state levels of the three proteins varied at different developmental stages. The results are discussed with respect to the physiological relevance in the plant organism.
Keywords
- Arabidopsis thaliana, Cyanide, Cysteine, Diurnal rhythm, Senescence, Sulfide, β-cyanoalanine
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Physiology
- Biochemistry, Genetics and Molecular Biology(all)
- Genetics
- Agricultural and Biological Sciences(all)
- Plant Science
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In: Plant physiology and biochemistry, Vol. 39, No. 10, 01.01.2001, p. 861-870.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Cysteine synthesis and cysteine desulfuration in Arabidopsis plants at different developmental stages and light conditions
AU - Burandt, P.
AU - Schmidt, A.
AU - Papenbrock, J.
N1 - Funding information: The expert technical assistance of P. von Trzebiatowski and Julia Volker is gratefully acknowledged. Many thanks to our gardeners for caring for the plants. We would like to thank Dr H. Hesse for giving us pCS-A, pCS-B and pCS-C cDNA clones. This work was financially supported by the Deutsche Forschungsgemeinschaft (PA 764/2-1, SCHM 307/15-1).
PY - 2001/1/1
Y1 - 2001/1/1
N2 - The last step in cysteine biosynthesis is catalysed by the pyridoxal 5′-phosphate-dependent enzyme O-acetyl-L-serine(thiol)lyase (OAS-TL). Several isoforms are localized in different compartments of the cell. OAS-TL and OAS-TL-like proteins also catalyse the formation of β-cyanoalanine and sulfide; the release of sulfide and of an unknown product was also observed. In Arabidopsis plants of different age, the OAS-TL activity decreased with increasing age whereas the enzymatical sulfide release from cysteine increased in older plants. The β-cyanoalanine synthase showed two activity peaks during the time course investigated. During a 12-h light/12-h dark rhythm, the OAS-TL and the sulfide-releasing activities ran parallel with a maximum in the light phase and a decrease of enzyme activity in the dark phase. β-Cyanoalanine synthase activities did not follow a special pattern. Three genes coding for the OAS-TL isoforms A, B, and C, which are presumably localized in the cytoplasm, in plastids, and in mitochondria, respectively, were differentially expressed. The mRNA steady-state levels of the three proteins varied at different developmental stages. The results are discussed with respect to the physiological relevance in the plant organism.
AB - The last step in cysteine biosynthesis is catalysed by the pyridoxal 5′-phosphate-dependent enzyme O-acetyl-L-serine(thiol)lyase (OAS-TL). Several isoforms are localized in different compartments of the cell. OAS-TL and OAS-TL-like proteins also catalyse the formation of β-cyanoalanine and sulfide; the release of sulfide and of an unknown product was also observed. In Arabidopsis plants of different age, the OAS-TL activity decreased with increasing age whereas the enzymatical sulfide release from cysteine increased in older plants. The β-cyanoalanine synthase showed two activity peaks during the time course investigated. During a 12-h light/12-h dark rhythm, the OAS-TL and the sulfide-releasing activities ran parallel with a maximum in the light phase and a decrease of enzyme activity in the dark phase. β-Cyanoalanine synthase activities did not follow a special pattern. Three genes coding for the OAS-TL isoforms A, B, and C, which are presumably localized in the cytoplasm, in plastids, and in mitochondria, respectively, were differentially expressed. The mRNA steady-state levels of the three proteins varied at different developmental stages. The results are discussed with respect to the physiological relevance in the plant organism.
KW - Arabidopsis thaliana
KW - Cyanide
KW - Cysteine
KW - Diurnal rhythm
KW - Senescence
KW - Sulfide
KW - β-cyanoalanine
UR - http://www.scopus.com/inward/record.url?scp=0034775705&partnerID=8YFLogxK
U2 - 10.1016/S0981-9428(01)01305-5
DO - 10.1016/S0981-9428(01)01305-5
M3 - Article
AN - SCOPUS:0034775705
VL - 39
SP - 861
EP - 870
JO - Plant physiology and biochemistry
JF - Plant physiology and biochemistry
SN - 0981-9428
IS - 10
ER -