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. 2011 Nov 16;63(3):1215–1224. doi: 10.1093/jxb/err346

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© 2011 The Author(s)

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details)

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Fig. 6. — Phosphorylation of the ACA8 N-terminus by different isoforms of CDPK. The N-terminus of WT ACA8 (6His-¹M-I¹¹⁶) was phosphorylated with Ca²⁺-independent mutants of A. thaliana CPK1 or CPK16 as described in the Materials and methods. Samples were solubilized and aliquots corresponding to 3 μg of 6His-¹M-I¹¹⁶ were subjected to SDS–PAGE, blotting, and autoradiography (lane 1, 6His-¹M-I¹¹⁶; lane 2, CPK1; lane 3, 6His-¹M-I¹¹⁶ plus CPK1; lane 4, CPK16; lane 5, 6His-¹M-I¹¹⁶ plus CPK16). Results are from one experiment representative of four.