Abstract
The activities of RNases and nucleases in wheat leaves are subject to control by stresses such as heat shock and prolonged darkness. Examination of one 27 kDa RNase revealed that heat shock resulted in a reduction of its activity without altering the level of the protein, suggesting post-translational control. During dark-induced senescence, all RNase and nuclease activities increase and the increase in 27 kDa RNase activity is controlled by ethylene. Examination of the 27 kDa RNase revealed that the increase in its activity was not accompanied by an increase in the level of the protein. Two-dimensional RNase activity gels and western analysis demonstrated that the 27 kDa RNase exists as multiple isoforms and that the activity of all isoforms increases during dark-induced senescence. These observations demonstrate that the increase in 27 kDa RNase activity is controlled post-translationally but is not achieved through changes in its isoelectric state.
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© 1999 Springer Science+Business Media Dordrecht
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Gallie, D.R., Chang, SC. (1999). RNase Activity is Post-Translationally Controlled During the Dark-Induced Senescence Program. In: Kanellis, A.K., Chang, C., Klee, H., Bleecker, A.B., Pech, J.C., Grierson, D. (eds) Biology and Biotechnology of the Plant Hormone Ethylene II. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4453-7_40
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DOI: https://doi.org/10.1007/978-94-011-4453-7_40
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