Two distinct regions of the murine p53 primary amino acid sequence are implicated in stable complex formation with simian virus 40 T antigen.
AUTOR(ES)
Jenkins, J R
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=253543Documentos Relacionados
- The p53 complex from monkey cells modulates the biochemical activities of simian virus 40 large T antigen.
- Identification of the p53 protein domain involved in formation of the simian virus 40 large T-antigen-p53 protein complex.
- Distinct residues of human p53 implicated in binding to DNA, simian virus 40 large T antigen, 53BP1, and 53BP2.
- Expression and complex formation of simian virus 40 large T antigen and mouse p53 in insect cells.
- Complex formation of simian virus 40 large T antigen with cellular protein p53.