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. 2023 Jan 19;24(3):2033. doi: 10.3390/ijms24032033

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© 2023 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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Asl preferentially binds to the PP5-dephosphorylated form of Plk4. Immobilized MBP-Plk4-TE was non-treated (lane 5) or treated with λ-phosphatase (λPPase, lane 3), GST-PP5 (lane 4) or GST-PP5^H326N (lane 6), respectively, and tested for binding to ³⁵S-Asl synthesized in IVTT reaction. MBP-Plk4-TE co-expressed with either His₆-PP5 (wild type) or His₆-PP5^H326N (inactive) in bacteria were immobilized to amylose resin and incubated with ³⁵S-Asl (lane 7–8). The in vitro binding assay reveals that dephosphorylated MBP-Plk4-TE binds more Asl, while the self-phosphorylated kinase binds less Asl. MBP was used as the negative control (lane 2). “p-” refers to phosphorylated Plk4. Coomassie-stained gel shows the loading and shifting of MBP-Plk4-TE derivatives. Short (1 h) and long (10 h) exposures of the autoradiographs are presented.