Modulation of mRNA stability by regulatory cis-acting AU-rich elements (AREs) and ARE-binding proteins is an important posttranscriptional mechanism of gene expression control. We previously demonstrated that the 3-untranslated region of BCL-2 mRNA contains an ARE that accounts for rapid BCL-2 down-regulation in response to apoptotic stimuli. We also demonstrated that the BCL-2 ARE core interacts with a number of AREbinding proteins, one of which is AU-rich factor 1/heterogeneous nuclear ribonucleoprotein D, known for its interaction with mRNA elements of others genes. In an attempt to search for other BCL-2 mRNA-binding proteins, we used the yeast RNA three-hybrid system assay and identified a novel human protein that interacts with BCL-2 ARE. We refer to it as TINO. The predicted protein sequence of TINO reveals two amino-terminal heterogeneous nuclear ribonucleoprotein K homology motifs for nucleic acid binding and a carboxyl-terminal RING domain, endowed with a putative E3 ubiquitinprotein ligase activity. In addition the novel protein is evolutionarily conserved; the two following orthologous proteins have been identified with protein-protein

Identification of Tino: a new evolutionarily conserved bcl-2 AU-rich element RNA binding protein / M.Donnini; A.Lapucci; L.Papucci; E.Witort; A.Jacquier; G.Brewer; A.Nicolin; S.Capaccioli; N.Schiavone. - In: THE JOURNAL OF BIOLOGICAL CHEMISTRY. - ISSN 0021-9258. - STAMPA. - 279:(2004), pp. 20154-20166. [10.1074/jbc.M314071200]

Identification of Tino: a new evolutionarily conserved bcl-2 AU-rich element RNA binding protein

DONNINI, MARTINO;LAPUCCI, ANDREA;PAPUCCI, LAURA;WITORT, EWA JANINA;CAPACCIOLI, SERGIO;SCHIAVONE, NICOLA
2004

Abstract

Modulation of mRNA stability by regulatory cis-acting AU-rich elements (AREs) and ARE-binding proteins is an important posttranscriptional mechanism of gene expression control. We previously demonstrated that the 3-untranslated region of BCL-2 mRNA contains an ARE that accounts for rapid BCL-2 down-regulation in response to apoptotic stimuli. We also demonstrated that the BCL-2 ARE core interacts with a number of AREbinding proteins, one of which is AU-rich factor 1/heterogeneous nuclear ribonucleoprotein D, known for its interaction with mRNA elements of others genes. In an attempt to search for other BCL-2 mRNA-binding proteins, we used the yeast RNA three-hybrid system assay and identified a novel human protein that interacts with BCL-2 ARE. We refer to it as TINO. The predicted protein sequence of TINO reveals two amino-terminal heterogeneous nuclear ribonucleoprotein K homology motifs for nucleic acid binding and a carboxyl-terminal RING domain, endowed with a putative E3 ubiquitinprotein ligase activity. In addition the novel protein is evolutionarily conserved; the two following orthologous proteins have been identified with protein-protein
2004
279
20154
20166
M.Donnini; A.Lapucci; L.Papucci; E.Witort; A.Jacquier; G.Brewer; A.Nicolin; S.Capaccioli; N.Schiavone
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/356837
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