Chène P
Oncology Department, Novartis, Basel, CH-4002, Switzerland.
J Mol Biol. 1999 May 21;288(5):883-90. doi: 10.1006/jmbi.1999.2734.
The p53 proteins from human, murine and Xenopus laevis are tetrameric. Previous work has shown that both human and murine p53 can form heterotetramers. However, despite a very high level of sequence homology at their tetramerisation domain, the human and the X. laevis p53 do not form heterooligomers. It is shown here that when inserted in the human p53 protein, the X. laevis tetramerisation domain is able to oligomerise with the human one. This indicates that the inability of X. laevis p53 to heterooligomerise with human p53 is due to another structural difference. The use of N and C-truncated X. laevis p53 proteins reveals that the deletion of the N terminus favours from the heterooligomerisation between the human and the X. laevis p53. The oligomerisation of the X. laevis p53 with the human protein is also enhanced when the N terminus of the X. laevis p53 is replaced by the human one. Altogether these data suggest that the N terminus of p53 influences the oligomerisation.
来自人类、小鼠和非洲爪蟾的p53蛋白是四聚体。先前的研究表明，人类和小鼠的p53都能形成异源四聚体。然而，尽管人类和非洲爪蟾的p53在其四聚化结构域具有非常高的序列同源性，但它们并不形成异源寡聚体。本文表明，当非洲爪蟾的四聚化结构域插入人类p53蛋白中时，它能够与人类的四聚化结构域形成寡聚体。这表明非洲爪蟾p53不能与人类p53形成异源寡聚体是由于另一种结构差异。使用N端和C端截短的非洲爪蟾p53蛋白表明，N端的缺失有利于人类和非洲爪蟾p53之间的异源寡聚化。当非洲爪蟾p53的N端被人类的N端取代时，非洲爪蟾p53与人类蛋白的寡聚化也会增强。总之，这些数据表明p53的N端会影响寡聚化。
