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. 2017 Mar 10;292(17):6952–6964. doi: 10.1074/jbc.M117.776468

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© 2017 by The American Society for Biochemistry and Molecular Biology, Inc.

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Figure 5. — Phosphorylation of the A-domain by KOC1 and its presence in TOC159. A, TOC159A was incubated with KOC1 isolated from NTAP-KOC1:koc1-1 plants (lane 1) or the same but heat-denatured KOC1 (De-KOC1) (lane 4) in the presence of [γ-³³P]ATP. B, purified TOC159A was incubated with [γ-³³P]ATP and with recombinant full-length KOC1 purified from bacteria (lane 3). C, purified TOC120A (lane 2) and TOC132A (lane 3) were incubated with [γ-³³P]ATP and KOC1 isolated from NTAP-KOC1:koc1-1 plants. In A–C, the samples were separated by SDS-PAGE and analyzed using a phosphorimaging system (Molecular Imager FX) and Quantity One 4.6 software. KOC1, TOC159A, TOC120A, and TOC132A were incubated alone with [γ-³³P]ATP as negative controls. D, total protein extracts of seedlings ppi2 (lane 1), WT (lane 2), NTAP-TOC159:ppi2 (lane 3), and NTAP-TOC159-cmyc:ppi2 (lane 4) were analyzed by Western blotting. The membrane was consecutively probed with antibodies against c-myc and rabbit IgG. The data shown are representative experiments of several replicates.