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.
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.
Soussi
T
T
Unité d'Oncologie Moléculaire, Institut de Recherches Scientifiques sur le Cancer, Villejuif, France.
Caron de Fromentel
C
C
Stürzbecher
H W
HW
Ullrich
S
S
Jenkins
J
J
May
P
P
D000818:Animals; D000952:Antigens, Polyomavirus Transforming / Q000378:metabolism*; D005075:Biological Evolution; D002460:Cell Line; D006360:Heat-Shock Proteins / Q000378:metabolism*; D009363:Neoplasm Proteins / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism*; D013696:Temperature; D014162:Transfection; D016159:Tumor Suppressor Protein p53; D014982:Xenopus laevis
D000952:Antigens, Polyomavirus Transforming; D006360:Heat-Shock Proteins; D009363:Neoplasm Proteins; D010750:Phosphoproteins; D016159:Tumor Suppressor Protein p53