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Title: Evidence for the interaction of the regulatory protein Ki-1/57 with p53 and its interacting proteins

Abstract

Ki-1/57 is a cytoplasmic and nuclear phospho-protein of 57 kDa and interacts with the adaptor protein RACK1, the transcription factor MEF2C, and the chromatin remodeling factor CHD3, suggesting that it might be involved in the regulation of transcription. Here, we describe yeast two-hybrid studies that identified a total of 11 proteins interacting with Ki-1/57, all of which interact or are functionally associated with p53 or other members of the p53 family of proteins. We further found that Ki-1/57 is able to interact with p53 itself in the yeast two-hybrid system when the interaction was tested directly. This interaction could be confirmed by pull down assays with purified proteins in vitro and by reciprocal co-immunoprecipitation assays from the human Hodgkin analogous lymphoma cell line L540. Furthermore, we found that the phosphorylation of p53 by PKC abolishes its interaction with Ki-1/57 in vitro.

Authors:
 [1];  [2];  [1];  [2];  [1];  [3]
  1. Centro de Biologia Molecular Estrutural, Laboratorio Nacional de Luz Sincrotron, Rua Giuseppe Maximo Scolfaro 10.000, C.P. 6192, 13084-971 Campinas, SP (Brazil)
  2. (Brazil)
  3. Centro de Biologia Molecular Estrutural, Laboratorio Nacional de Luz Sincrotron, Rua Giuseppe Maximo Scolfaro 10.000, C.P. 6192, 13084-971 Campinas, SP (Brazil) and Departamento de Genetica e Evolucao, Universidade Estadual de Campinas, Campinas, SP (Brazil) and Departamento de Bioquimica, Universidade Estadual de Campinas, Campinas, SP (Brazil). E-mail: jkobarg@lnls.br
Publication Date:
OSTI Identifier:
20798846
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 341; Journal Issue: 3; Other Information: DOI: 10.1016/j.bbrc.2006.01.036; PII: S0006-291X(06)00103-3; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; CHROMATIN; HYBRID SYSTEMS; IN VITRO; LYMPHOMAS; PHOSPHORYLATION; TRANSCRIPTION; TRANSCRIPTION FACTORS; YEASTS

Citation Formats

Nery, Flavia C., Departamento de Genetica e Evolucao, Universidade Estadual de Campinas, Campinas, SP, Rui, Edmilson, Departamento de Bioquimica, Universidade Estadual de Campinas, Campinas, SP, Kuniyoshi, Tais M., and Kobarg, Joerg. Evidence for the interaction of the regulatory protein Ki-1/57 with p53 and its interacting proteins. United States: N. p., 2006. Web. doi:10.1016/j.bbrc.2006.01.036.
Nery, Flavia C., Departamento de Genetica e Evolucao, Universidade Estadual de Campinas, Campinas, SP, Rui, Edmilson, Departamento de Bioquimica, Universidade Estadual de Campinas, Campinas, SP, Kuniyoshi, Tais M., & Kobarg, Joerg. Evidence for the interaction of the regulatory protein Ki-1/57 with p53 and its interacting proteins. United States. doi:10.1016/j.bbrc.2006.01.036.
Nery, Flavia C., Departamento de Genetica e Evolucao, Universidade Estadual de Campinas, Campinas, SP, Rui, Edmilson, Departamento de Bioquimica, Universidade Estadual de Campinas, Campinas, SP, Kuniyoshi, Tais M., and Kobarg, Joerg. Fri . "Evidence for the interaction of the regulatory protein Ki-1/57 with p53 and its interacting proteins". United States. doi:10.1016/j.bbrc.2006.01.036.
@article{osti_20798846,
title = {Evidence for the interaction of the regulatory protein Ki-1/57 with p53 and its interacting proteins},
author = {Nery, Flavia C. and Departamento de Genetica e Evolucao, Universidade Estadual de Campinas, Campinas, SP and Rui, Edmilson and Departamento de Bioquimica, Universidade Estadual de Campinas, Campinas, SP and Kuniyoshi, Tais M. and Kobarg, Joerg},
abstractNote = {Ki-1/57 is a cytoplasmic and nuclear phospho-protein of 57 kDa and interacts with the adaptor protein RACK1, the transcription factor MEF2C, and the chromatin remodeling factor CHD3, suggesting that it might be involved in the regulation of transcription. Here, we describe yeast two-hybrid studies that identified a total of 11 proteins interacting with Ki-1/57, all of which interact or are functionally associated with p53 or other members of the p53 family of proteins. We further found that Ki-1/57 is able to interact with p53 itself in the yeast two-hybrid system when the interaction was tested directly. This interaction could be confirmed by pull down assays with purified proteins in vitro and by reciprocal co-immunoprecipitation assays from the human Hodgkin analogous lymphoma cell line L540. Furthermore, we found that the phosphorylation of p53 by PKC abolishes its interaction with Ki-1/57 in vitro.},
doi = {10.1016/j.bbrc.2006.01.036},
journal = {Biochemical and Biophysical Research Communications},
number = 3,
volume = 341,
place = {United States},
year = {Fri Mar 17 00:00:00 EST 2006},
month = {Fri Mar 17 00:00:00 EST 2006}
}