期刊
FEBS LETTERS
卷 549, 期 1-3, 页码 63-66出版社
WILEY
DOI: 10.1016/S0014-5793(03)00770-1
关键词
piD261/Bud32; protein kinase; protein phosphorylation; surface plasmon resonance; p53; Saccharomyces cerevisiae
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. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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