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Figure 7
Assessing a putative kinase activity of the KaiCI domain. SDS–PAGE assay of the phosphorylation status of full-length S. elongatus KaiC (KaiC), KaiC treated with λ phosphatase (λPP), S. elongatus KaiCI (wt-KaiCI), the S. elongatus KaiCI triple mutant A192T/E197S/E198T (TST-KaiCI) and S. elongatus KaiCII (KaiCII). Residue numberings between CI from S. elongatus and T. elongatus differ by one, i.e. S. elongatus mutations A192T/E197S/E198T correspond to T. elongatus mutations A193T/E198S/E199T. Multiple bands for KaiC and the double band for KaiCII represent the phosphorylated (top) and nonphosphorylated (bottom) states. In contrast, single bands for wt-­KaiCI and TST-KaiCI indicate that neither protein is phosphorylated. That KaiCII expressed as a separate domain still exhibits phosphorylation despite its inability to form stable hexamers has previously been demonstrated (Pattanayek et al., 2008BB41).

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
Volume 70| Part 5| May 2014| Pages 1375-1390
https://doi.org/10.1107/S1399004714003228
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