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Updated: Sep 20, 2026

Yeast As a Chassis for Developing Functional Assays to Study Human P53
Published on: August 4, 2019
Functional homology between yeast piD261/Bud32 and human PRPK: both phosphorylate p53 and PRPK partially complements
Sonia Facchin1, Raffaele Lopreiato, Maria Ruzzene
1Dipartimento di Chimica Biologica, Università di Padova, Viale G Colombo 3, 35121 Padova, Italy.
Abstract:
Yeast piD261/Bud32 belongs to the piD261 family of atypical protein kinases structurally conserved, from Archaea to human. The disruption of its gene is causative of severely defective growth. Its human homologue, PRPK, interacts with and phosphorylates the oncosuppressor p53 protein, which is lacking in yeast. Here we show that on one hand piD261/Bud32 interacts with and phosphorylates human p53 in vitro, on the other hand PRPK can partially complement the phenotype of yeast lacking the gene encoding piD261/Bud32. These data indicate that, despite considerable structural divergence, members of the piD261 family from distantly related organisms display a remarkable functional conservation.
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