By using a novel genetic approach, based on the properties of lambda cl repressor, we demonstrate that the HIV-1 Tat protein specifically interacts with the human p53 protein via the p53 O2 dimerization domain. By random and site-specific mutagenesis, we also identify the residues in Tat and O2 peptides which are involved in this interaction. Two alternative biological consequences are expected to result from Tat-p53 interaction: (i) Tat-O2 interaction inactivates p53 regulation function, thus producing cell transformation; (ii) Tat-O2 interaction favours the formation of p53 dimers, thus leading the cell towards apoptosis. (C) 1995 Academic Press, Inc.

Longo F., M.M. (1995). A novel approach to protein-protein interaction: Complex formation between the p53 tumor suppressor and the HIV Tat proteins. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 206(1), 326-334 [10.1006/bbrc.1995.1045].

A novel approach to protein-protein interaction: Complex formation between the p53 tumor suppressor and the HIV Tat proteins

CASTAGNOLI, LUISA;
1995

Abstract

By using a novel genetic approach, based on the properties of lambda cl repressor, we demonstrate that the HIV-1 Tat protein specifically interacts with the human p53 protein via the p53 O2 dimerization domain. By random and site-specific mutagenesis, we also identify the residues in Tat and O2 peptides which are involved in this interaction. Two alternative biological consequences are expected to result from Tat-p53 interaction: (i) Tat-O2 interaction inactivates p53 regulation function, thus producing cell transformation; (ii) Tat-O2 interaction favours the formation of p53 dimers, thus leading the cell towards apoptosis. (C) 1995 Academic Press, Inc.
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/18 - Genetica
English
Con Impact Factor ISI
protein p53; transactivator protein; apoptosis; article; cell transformation; complex formation; dimerization; human; human immunodeficiency virus 1; nonhuman; priority journal; protein protein interaction; site directed mutagenesis; Amino Acid Sequence; Comparative Study; Gene Products, tat; HIV-1; Macromolecular Systems; Molecular Sequence Data; Mutagenesis; Mutagenesis, Site-Directed; Plasmids; Protein Hybridization; Protein p53; Protein Structure, Secondary; Random Allocation; Recombinant Proteins; Repressor Proteins; Restriction Mapping; Support, Non-U.S. Gov't; Human immunodeficiency virus; Human immunodeficiency virus 1
Longo F., M.M. (1995). A novel approach to protein-protein interaction: Complex formation between the p53 tumor suppressor and the HIV Tat proteins. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 206(1), 326-334 [10.1006/bbrc.1995.1045].
Longo, F; Marchetti, Ma; Castagnoli, L; Battaglia, Pa; Gigliani, F
Articolo su rivista
File in questo prodotto:
File Dimensione Formato  
Longo 1995.pdf

accesso aperto

Descrizione: Articolo principale
Dimensione 479.56 kB
Formato Adobe PDF
479.56 kB Adobe PDF Visualizza/Apri

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2108/53244
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 54
  • ???jsp.display-item.citation.isi??? 51
social impact