Two distinct regions of the murine p53 primary amino acid sequence are implicated in stable complex formation with simian virus 40 T antigen.
We mapped regions of the mouse p53 primary amino acid sequence implicated in stable complex formation with simian virus 40 T antigen. A number of mutant p53 proteins failed to complex stably with T antigen in vivo but formed stable complexes with T antigen in in vitro association assays. In contrast to an earlier report (T.-H. Tan, H. Wallis, and A. J. Levine, J. Virol. 59:574-583, 1986), our study showed that two distinct regions of p53 primary amino acid sequence, highly conserved between mouse and Xenopus laevis, were implicated in stable complex formation. Our data support the proposal that, when in complex, T antigen may occupy a site on p53 that is implicated in the normal function of the protein.
D000595:Amino Acid Sequence; D000818:Animals; D000952:Antigens, Polyomavirus Transforming / Q000378:metabolism*; D002461:Cell Line, Transformed; D051379:Mice; D009154:Mutation; D009363:Neoplasm Proteins / Q000235:genetics / Q000378:metabolism*; D010750:Phosphoproteins / Q000235:genetics / Q000378:metabolism*; D011233:Precipitin Tests; D014162:Transfection; D016159:Tumor Suppressor Protein p53
D000952:Antigens, Polyomavirus Transforming; D009363:Neoplasm Proteins; D010750:Phosphoproteins; D016159:Tumor Suppressor Protein p53