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Papers In Press, published online ahead of print February 9, 2004
Department of Experimental Pathology and Oncology, University of Florence, Florence, Italy 50134
Corresponding Author: sergio{at}unifi.it
Modulation of mRNA stability by regulatory cis-acting AU-rich elements (ARE) and ARE binding proteins (AUBPs) 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 downregulation in response to apoptotic stimuli. We also demonstrated that the bcl-2 ARE core interacts with a number of AUBPs, one of which is AUF1/hnRNP 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 (RNA THS) 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 N-terminal hnRNP K homology motifs (KH) for nucleic acid binding and a C-terminal RING domain, endowed with a putative E3 ubiquitin-protein ligase activity. In addition the novel protein is evolutionarily conserved; the two following orthologous proteins have been identified with protein-protein BLAST: PEM-3 of Ciona savignyi and MEX-3 of Caenorhabditis elegans. Upon binding, Tino destabilizes a chimeric reporter construct containing the bcl-2 ARE sequence, revealing a negative regulatory action on bcl-2 gene expression at the posttranscriptional level.
J. Biol. Chem, 10.1074/jbc.M314071200
Submitted on December 23, 2003
Revised on February 2, 2004
Accepted on February 9, 2004
Identification of Tino: A new evolutionarily conserved bcl-2 AU-rich element RNA binding protein
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