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Activation of p53 by conjugation to the ubiquitin‐like protein SUMO‐1
Author(s) -
Gostissa Monica,
Hengstermann Arnd,
Fogal Valentina,
Sandy Peter,
Schwarz Sylvia E.,
Scheffner Martin,
Del Sal Giannino
Publication year - 1999
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/18.22.6462
Subject(s) - sumo protein , sumo enzymes , biology , ubiquitin , transactivation , lysine , biochemistry , microbiology and biotechnology , ubiquitins , in vitro , amino acid , ubiquitin ligase , transcription factor , gene
The growth‐suppressive properties of p53 are controlled 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.