A versatile strategy to define the phosphorylation preferences of plant protein kinases and screen for putative substrates
Article first published online: 28 JUN 2008
© 2008 The Authors. Journal compilation © 2008 Blackwell Publishing Ltd
The Plant Journal
Volume 55, Issue 1, pages 104–117, July 2008
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
- Issue published online: 28 JUN 2008
- Article first published online: 28 JUN 2008
- Received 15 November 2007; revised 28 February 2008; accepted 6 March 2008; published online 20 May 2008.
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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