TAILIEUCHUNG - Báo cáo khoa học: Genomic structure and expression analysis of the RNase j family ortholog gene in the insect Ceratitis capitata

Cc RNase is the founding member of the recently identified RNasej family, which is represented by a single ortholog in a wide range of animal taxonomic groups. Although the precise biological role of this protein is still unknown, it has been shown that the recombinant proteins isolated so far from the insect Ceratitis capitataand from human exhibit ribonucleo-lytic activity. | ỊFEBS Journal Genomic structure and expression analysis of the RNase K family ortholog gene in the insect Ceratitis capitata Theodores N. Rampias Emmanuel G. Fragoulis and Diamantis C. Sideris Department of Biochemistry and Molecular Biology Faculty of Biology University of Athens Greece Keywords alternative polyadenylation AUUUA motifs Cc RNase RNase k specific ribonuclease Correspondence D. C. Sideris Department of Biochemistry and Molecular Biology Faculty of Biology University of Athens Panepistimioupolis 15701 Athens Greece Fax 30 210 7274158 Tel 30 210 7274515 E-mail dsideris@ Present address Department of Molecular Biophysics and Biochemistry Yale University New Haven CT USA Database The nucleotide sequences of Ceratitis capi-tata RNase k have been submitted to the DDBJ EMBL GenBank databases under the accession numbers AJ874689 cDNA and AJ874690 genomic DNA Received 28 July 2008 revised 9 September 2008 accepted 16 October 2008 doi Cc RNase is the founding member of the recently identified RNase k family which is represented by a single ortholog in a wide range of animal taxonomic groups. Although the precise biological role of this protein is still unknown it has been shown that the recombinant proteins isolated so far from the insect Ceratitis capitata and from human exhibit ribonucleo-lytic activity. In this work we report the genomic organization and molecular evolution of the RNase k gene from various animal species as well as expression analysis of the ortholog gene in C. capitata. The high degree of amino acid sequence similarity in combination with the fact that exon sizes and intronic positions are extremely conserved among RNase k orthologs in 15 diverse genomes from sea anemone to human imply a very significant biological function for this enzyme. In C. capitata two forms of RNase k mRNA and kb with various lengths of 3 UTR were identified as alternative products of a single gene resulting from

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