TAILIEUCHUNG - Báo cáo khoa học: In vitro embryonic developmental phosphorylation of the cellular nucleic acid binding protein by cAMP-dependent protein kinase, and its relevance for biochemical activities

The zinc-finger cellular nucleic acid binding protein (CNBP) is a strikingly conserved single-stranded nucleic acid binding protein essential for normal forebrain formation during mouse and chick embryogenesis. CNBP cDNAs from a number of vertebrates have been cloned and analysed. CNBP is mainly conformed by seven retroviral Cys-Cys-His-Cys zinc-knuckles and a glycine⁄arginine rich region box. | ỊFEBS Journal In vitro embryonic developmental phosphorylation of the cellular nucleic acid binding protein by cAMP-dependent protein kinase and its relevance for biochemical activities Veronica A. Lombardo Pablo Armas Andrea M. J. Weiner and Nora B. Calcaterra Division Biología delDesarrollo IBR - CONICET Area Biologia General Facultad de Ciencias Bioquimicas y Farmaceuticas Universidad Nacionalde Rosario Argentina Keywords CNBP Danio rerio embryogenesis phosphorylation PKA Correspondence N. B. Calcaterra IBR - CONICET Area Biologia General Dpto. de Ciencias Biologicas Facultad de Ciencias Bioquimicas y Farmaceuticas Universidad Nacionalde Rosario Suipacha 531 S2002LRK Rosario Argentina Tel Fax 54 341 4804601 E-mail calcaterra@ or ncalcate@ Database CNBPS158A nucleotide sequence data is available in the GenBank database under the accession number DQ519386 Received 9 October 2006 revised 6 November 2006 accepted 15 November 2006 doi The zinc-finger cellular nucleic acid binding protein CNBP is a strikingly conserved single-stranded nucleic acid binding protein essential for normal forebrain formation during mouse and chick embryogenesis. CNBP cDNAs from a number of vertebrates have been cloned and analysed. CNBP is mainly conformed by seven retroviral Cys-Cys-His-Cys zinc-knuckles and a glycine arginine rich region box. CNBP amino acid sequences show a putative Pro-Glu-Ser-Thr site of proteolysis and several putative phosphorylation sites. In this study we analysed CNBP phosphorylation by embryonic kinases and its consequences on CNBP biochemical activities. We report that CNBP is differentially phosphorylated by Danio rerio embryonic extracts. In vitro CNBP phosphorylation is basal and constant at early embryonic developmental stages it begins to increase after mid-blastula transition stage reaching the highest level at 48 hours postfertilization stage and decreases thereafter to basal levels at 5 days .

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