Tools to investigate reaction oxygen species-sensitive signaling proteins

Desikan, R., Neill, S., Slinn, J. and Hancock, J. T. (2009) Tools to investigate reaction oxygen species-sensitive signaling proteins. In: Hancock, J. T., ed. (2009) Redox-Mediated Signal Transduction. (476) Humana Press, pp. 84-96. ISBN 978-1-58829-842-3 Available from:

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The thiols groups of cysteine residues on proteins are attractive oxidative targets for modification by reactive oxygen species, such as hydrogen peroxide (H2O2). Such modification can lead to important cellular signaling processes that ultimately result in modification of physiology of the organism. To identify such proteins that are amenable to oxidative modification, different methods can be used. Here, two such approaches are described: one being the use of fluorescent thiol derivatives, and the second being the use of genetic mutants that are mutated in thiol residues. Using the model plant Arabidopsis thaliana, cell cultures, and whole plants, we describe these tools to help the reader understand the function of such thiol modification on plant responses.

Item Type:Book Section
Uncontrolled Keywords:glyceraldehyde 3-phosphate dehydrogenase, histidine kinase, hydrogen peroxide, 5′-iodoacetamide fluorescein, reactive oxygen species, stomatal guard cells, thiol labeling
Faculty/Department:Faculty of Health and Applied Sciences > Department of Applied Sciences
ID Code:7094
Deposited By: H. Hammond
Deposited On:22 Jul 2010 07:50
Last Modified:15 Nov 2016 20:58

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