Characterisation of the interface between nucleophosmin (NPM) and p53: Potential role in p53 stabilisation

被引：33

作者：

Lambert, B ^{[1
]}

Buckle, M ^{[1
]}

机构：

[1] Ecole Normale Super, CNRS, LBPA, UMR 8113, F-94235 Cachan, France

来源：

FEBS LETTERS | 2006年 / 580卷 / 01期

关键词：

nucleophosmin; p53; stabilisation; interaction domains; chemical cross-linking; peptide analysis; SELDI;

D O I：

10.1016/j.febslet.2005.12.025

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

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. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：345 / 350

页数：6

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