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J Virol September 1, 1989; 63 (9): 3894-901.
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Evolutionary conservation of the biochemical properties of p53: specific interaction of Xenopus laevis p53 with simian virus 40 large T antigen and mammalian heat shock proteins 70.

Soussi T , Caron de Fromentel C , Stürzbecher HW , Ullrich S , Jenkins J , May P .

We have investigated the biochemical properties of Xenopus laevis p53. With an in vitro binding assay, we can detect a specific association between X. laevis p53 and simian virus 40 large T antigen. Furthermore, X. laevis p53 expressed in monkey COS cells is stably associated with this viral antigen. Like mammalian p53, X. laevis p53 in complex with simian virus 40 large T antigen exhibits a 20-fold increase of its half-life. On the other hand, X. laevis p53 is unable to associate either in vivo or in vitro with adenovirus type 5 E1B 55-kilodalton protein. We show by an immunological technique that X. laevis p53 forms specific complexes with mammalian hsp72 and hsp73 heat shock proteins only at a temperature well above the optimal growth temperature for X. laevis. Our results suggest that the protein-binding properties of p53 are closely related to the functional activity of the protein.

PubMed ID: 2668561
PMC ID: PMC250985
Article link: J Virol

Species referenced: Xenopus laevis
Genes referenced: hspa1a hspa8 tp53

References [+] :
Benoist, Deletions covering the putative promoter region of early mRNAs of simian virus 40 do not abolish T-antigen expression. 1981, Pubmed