Facchin Sonia, Lopreiato Raffaele, Ruzzene Maria, Marin Oriano, Sartori Geppo, Götz Claudia, Montenarh Mathias, Carignani Giovanna, Pinna Lorenzo A
Dipartimento di Chimica Biologica, Università di Padova, Viale G Colombo 3, 35121 Padova, Italy.
FEBS Lett. 2003 Aug 14;549(1-3):63-6. doi: 10.1016/s0014-5793(03)00770-1.
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.
酵母中的piD261/Bud32属于非典型蛋白激酶的piD261家族，从古细菌到人类，其结构具有保守性。该基因的破坏会导致严重的生长缺陷。它在人类中的同源物PRPK与肿瘤抑制蛋白p53相互作用并使其磷酸化，而酵母中不存在p53蛋白。在这里我们表明，一方面piD261/Bud32在体外与人类p53相互作用并使其磷酸化，另一方面PRPK可以部分弥补缺乏编码piD261/Bud32基因的酵母的表型。这些数据表明，尽管在结构上存在相当大的差异，但来自远缘生物的piD261家族成员仍表现出显著的功能保守性。
