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. 2019 Jul 8;9:9846. doi: 10.1038/s41598-019-46327-0

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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p23-1 phosphorylation by a monomeric 40-kDa CK2. (A) p23-1 (0.1 μg, lanes 1 and 2) was incubated with recombinant human monomeric CK2 (α, 15 ng) or tetrameric CK2 (α₂β₂, 5 ng); β-casein (1 μg, lanes 3 and 4) was used to ensure that the amount of each CK2 isoform chosen had the same catalytic activity towards a model substrate. After radioactive phosphorylation (10 min at 30 °C), samples were resolved by SDS-PAGE. A representative autoradiograph is shown. (B) Representative autoradiography of an in-gel kinase assay: 10 or 20 μg protein from Arabidopsis total extract (in duplicate, as indicated) was resolved by SDS-PAGE in which p23-1 (10 μg/ml) was included in the gel. In lane 1, human recombinant CK2 α (hsCK2α 50 ng, Mw 40 kDa) was loaded as a positive control. After electrophoresis and protein renaturation, the gel was incubated with a radioactive phosphorylation mixture and analyzed by autoradiography. The migration of Mw markers is shown on the left.