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A versatile strategy to define the phosphorylation preferences of plant protein kinases and screen for putative substrates

  1. Florina Vlad1,
  2. Benjamin E. Turk2,
  3. Philippe Peynot1,
  4. Jeffrey Leung1,
  5. Sylvain Merlot1,*

Article first published online: 28 JUN 2008

DOI: 10.1111/j.1365-313X.2008.03488.x

Issue

The Plant Journal

The Plant Journal

Volume 55, Issue 1, pages 104–117, July 2008

Additional Information

How to Cite

Vlad, F., Turk, B. E., Peynot, P., Leung, J. and Merlot, S. (2008), A versatile strategy to define the phosphorylation preferences of plant protein kinases and screen for putative substrates. The Plant Journal, 55: 104–117. doi: 10.1111/j.1365-313X.2008.03488.x

Author Information

  1. 1

    Centre National de la Recherche Scientifique, Institut des Sciences du Végétal, UPR 2355, 1 avenue de la Terrasse, Bât. 23, 91198 Gif-sur-Yvette Cedex, France, and

  2. 2

    Department of Pharmacology, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, USA

* * (fax +33 1 69823596; e-mail sylvain.merlot@isv.cnrs-gif.fr).

Publication History

  1. Issue published online: 28 JUN 2008
  2. Article first published online: 28 JUN 2008
  3. Received 15 November 2007; revised 28 February 2008; accepted 6 March 2008; published online 20 May 2008.

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Figure  S1. Purification of active CDPK–SnRK kinases from E.  coli protein extracts. Purified AKIN10, SnRK2-10, SOS2 and CDPK32 kinases (1–3 mg) were resolved on a SDS-PAGE gel and revealed with coomassie blue staining. Notice that SnRK2-10 migrates as a smear around 50 kDa probably due to the presence of multiple phosphorylated forms and some protein degradation.

Table  S1. Extended lists of CDPK32, AKIN10, SnRK2-10 and SOS2 putative substrates.

Appendix  S1. Formatted PSSM for CDPK32, AKIN10, SnRK2-10 and SOS2 (used to search the protein sequence databases using the MAST program).

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