Abstract
Programmed cell death (PCD) was induced by the Yariv reagent in Nicotiana tabacum cv. Bright Yellow-2 cell suspension. The analyses of proteins extracts by 2-D electrophoresis clearly show massive protein degradation which was mainly due to cysteine protease activity. In contrast, some proteins remained unchanged up to 72 h after PCD induction. Peptide mass fingerprints of these proteins, obtained by MALDI-TOF, identified calreticulin, heat shock protein (HSP) 60, HSP70, malate dehydrogenase and mitochondrial ATP synthase β-subunit.
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Abbreviations
- AGPs:
-
arabinogalactan-proteins
- ATPase:
-
ATP synthase β-subunit
- BY-2:
-
Bright Yellow-2
- CRT:
-
calreticulin
- 2;4-D:
-
2;4-dichlorophenoxyacetic acid
- 2-DE:
-
2-dimensional electrophoresis
- IEF:
-
isoelectric focusing
- HSP:
-
heat shock protein
- MALDI-TOF:
-
matrix assisted laser desorption/ionization-time of fight
- MS:
-
mass spectrometry
- MDH:
-
malatedehydrogenase
- MS medium:
-
Murashige and Skoog medium
- PCD:
-
programmed cell death
- TBP:
-
tributylphosphine
- TCA:
-
trichloroacetic acid
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Acknowledgements
We thank Dr. P. Jackson for the critical reading of the manuscript and Dr. M.J. Kieliszewski for generously providing the BY-2 suspension cultured cells. This research received financial support from Praxis XXI fellowship SFRH/BD/1183/2000.
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Chaves, I., Alves, M., Carrilho, D. et al. Protein changes during programmed cell death in tobacco. Biol Plant 55, 153–158 (2011). https://doi.org/10.1007/s10535-011-0021-y
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DOI: https://doi.org/10.1007/s10535-011-0021-y