Skip to main content

Tools to Investigate ROS Sensitive Signalling Proteins

  • Protocol
  • First Online:
Redox-Mediated Signal Transduction

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 476))

Abstract

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.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Protocol
USD 49.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 84.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 109.00
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 109.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

References

  1. Cooper, C., Patel, R. P., Brookes, P. S., and Darley-Usmar, V. M. (2002) Nanotransducers in cellular redox signalling: modification of thiols by reactive oxygen and reactive nitrogen species. Trends Biochem Sci 27, 489–492.

    Article  PubMed  CAS  Google Scholar 

  2. Hancock, J. T., Henson, D., Nyirenda, M., Desikan, R., Harrison, J., Lewis, M., Hughes, J., and Neill, S. J. (2005) Proteomic identification of glyceraldehyde 3-phosphate dehydrogenase as an inhibitory target of hydrogen peroxide in Arabidopsis. Plant Physiol Biochem. 43, 828–835.

    Article  PubMed  CAS  Google Scholar 

  3. Desikan, R., Hancock, J. T., Bright, J., Harrison, J., Weir, I., Hooley, R., and Neill, S. J. (2005) A novel role for ETR1: hydrogen peroxide signalling in stomatal guard cells. Plant Physiol 137, 831–834.

    Article  PubMed  CAS  Google Scholar 

  4. Pei, Z.-M., Murata, Y., Benning, G., Thomine, S., Klusener, B., Allen, G. J., Grill, E., and Schroeder, J. I. (2000) Calcium channels activated by hydrogen peroxide mediate abscisic acid signalling in guard cells. Nature 406, 731–734.

    Article  PubMed  CAS  Google Scholar 

  5. Foreman, J., Denidchik, V., Bothwell, J. H.F., Mylona, P., Miedema, H., Torres, M. A., Instead, P., Costa, S., Brownlee, C., Jones, J. D.G., Davies, J. M., and Dolan, L. (2003) Reactive oxygen species produced by NADPH oxidase regulate plant cell growth. Nature 422, 442–446.

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2008 Humana Press, a part of Springer Science+Business Media, LLC

About this protocol

Cite this protocol

Desikan, R., Neill, S.J., Slinn, J., Hancock, J.T. (2008). Tools to Investigate ROS Sensitive Signalling Proteins. In: Hancock, J.T. (eds) Redox-Mediated Signal Transduction. Methods in Molecular Biology™, vol 476. Humana Press. https://doi.org/10.1007/978-1-59745-129-1_7

Download citation

  • DOI: https://doi.org/10.1007/978-1-59745-129-1_7

  • Published:

  • Publisher Name: Humana Press

  • Print ISBN: 978-1-58829-842-3

  • Online ISBN: 978-1-59745-129-1

  • eBook Packages: Springer Protocols

Publish with us

Policies and ethics