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. 2018 Jul 1;29(13):1664–1674. doi: 10.1091/mbc.E18-02-0129

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© 2018 Elmore et al. “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology.

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FIGURE 2: — The C-termini of Hhp1/2 are dispensable for their functions. (A) Schematic diagrams of Hhp1/2 with relative positions of N-terminal extensions (N, green), kinase domains (blue), kinase domain extensions (KDE, yellow), and unrelated C-termini in red or purple indicated, drawn to scale. (B) Anti-GFP immunoblots of whole-cell extracts prepared from untagged and the indicated GFP-tagged strains. Anti-PSTAIRE (Cdc2) immunoblots served as protein loading controls. (C) Live-cell imaging of endogenously tagged Hhp1-(1-296)-GFP and Hhp2-(1-295)-GFP with Sid4-RFP. Scale bars: 5 µm. (D) Serial 10-fold dilutions of the indicated strains were spotted on YE plates and incubated at the indicated temperatures. (E) In vitro kinase assays of recombinant MBP-Hhp1, MBP-Hhp1-(1-296), MBP-Hhp2, and MBP-Hhp2-(1-295) detected by Coomassie blue (CB) staining of SDS–PAGE gels, with casein as substrate. Phosphorylated casein was detected by autoradiography (³²P). (F) Sid4 from the indicated strains was immunoprecipitated from denatured cell lysates, treated with phosphatase, and visualized by immunoblotting.