Activation of p53 by conjugation to the ubiquitin-like protein SUMO-1
Activation of p53 by conjugation to the ubiquitin-like protein SUMO-1
复制标题
DOI：
10.1093/emboj/18.22.6462
复制
发表时间：
1999-11-15
期刊：
影响因子：
11.4
通讯作者：
Del Sal, G
中科院分区：
文献类型：
--
作者：
Gostissa, M;Hengstermann, A;Del Sal, G
p53的生长抑制特性是由翻译后修饰和调节其周转率控制的。在这里，我们表明，p53可以在体外和体内修饰的小泛素样蛋白SUMO-1的共轭。p53的氨基酸位置386处的赖氨酸残基是这种先前未描述的修饰所必需的，强烈地表明该赖氨酸残基充当SUMO-1的主要附着位点。与泛素不同，SUMO-1的附着似乎不与靶蛋白快速降解，而是已经提出改变修饰的蛋白质与其他细胞蛋白质相互作用的能力。因此，我们提供了SUMO-1与野生型p53结合导致p53反式激活能力增加的证据。我们认为，SUMO-1共轭p53的翻译后修饰提供了一种新的机制来调节p53的活性。
The growth-suppressive properties of p53 are trolled by posttranslational modifications and by regulation of its turnover rate. Here we show that p53 can be modified in vitro and in vivo by conjugation to the small ubiquitin-like protein SUMO-1. A lysine residue at amino acid position 386 of p53 is required for this previously undescribed modification, strongly suggesting that this lysine residue serves as the major attachment site for SUMO-1, Unlike ubiquitin, attachment of SUMO-1 does not appear to target proteins for rapid degradation but rather, has been proposed to change the ability of the modified protein to interact with other cellular proteins. Accordingly, we provide evidence that conjugation of SUMO-1 to wild-type p53 results in an increased transactivation ability of p53. We suggest that posttranslational modification of p53 by SUMO-1 conjugation provides a novel mechanism to regulate p53 activity.