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. 2017 Mar 13;8:323. doi: 10.3389/fpls.2017.00323

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Copyright © 2017 Wu and Li.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Arabidopsis Ying Yang 1 can be phosphorylated by CKII in vitro and S²⁸⁴ is a major CKII phosphorylation site. (A) In vitro phosphorylation assay of wild-type and mutant AtYY1 proteins by CKII. Phosphorylated proteins were detected by immunoblotting with an anti-phosphoserine antibody. Identical protein loading amounts (3 μg) were confirmed by immunoblotting using an anti-His antibody. Relative phosphorylation signal intensity was labeled below each lane. (B) A typical phosphorylated peptide from AtYY1 identified by LC-MS/MS. S^P shows that the S²⁸⁴ site is phosphorylated. The fragment ions assigned to both y-ions and b-ions are labeled.