Characterisation of the interface between nucleophosmin (NPM) and p53: potential role in p53 stabilisation.
We have used surface plasmon resonance to quantify the kinetics and stoichiometry of the interaction between p53 and nucleophosmin (NPM). Domains characterising the interface between the two proteins were identified by chemical cross-linking, proteolytic digestion and mass spectrometry based peptide mapping. We show that the C-terminal domain of NPM (residues 242-269) interacts with two regions of p53 (residues 175-196 and residues 343-363) which belong, respectively, to the DNA binding domain and the tetramerisation domain. Potential biological consequences of such interactions are discussed.
Lambert
B
B
Enzymologie et Cinétique Structurale, LBPA, UMR 8113 CNRS/Ecole Normale Supérieure de Cachan, 61 Avenue du Président Wilson, 94235 Cachan, France. lambert@lbpa.ens-cachan.fr
Buckle
M
M
D000818:Animals; D006801:Humans; D046912:Multiprotein Complexes / Q000737:chemistry* / Q000378:metabolism; D009687:Nuclear Proteins / Q000737:chemistry* / Q000378:metabolism; D000090243:Nucleophosmin; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D020349:Surface Plasmon Resonance; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry* / Q000378:metabolism
D046912:Multiprotein Complexes; C000716967:NPM1 protein, human; D009687:Nuclear Proteins; D016159:Tumor Suppressor Protein p53; D000090243:Nucleophosmin