Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học Minireview cung cấp cho các bạn kiến thức về ngành y đề tài: Molecular evolution of neuropeptides in the genus Drosophila. | Open Access Research Molecular evolution of neuropeptides in the genus Drosophila Christian Wegener and Anton Gorbashov Address Emmy Noether Neuropeptide Group Animal Physiology Department of Biology Philipps-University Karl-von-Frisch-Strasse D35032 Marburg Germany. Correspondence Christian Wegener. Email wegener@ Published 21 August 2008 Genome Biology 2008 9 R131 doi gb-2008-9-8-rl3l The electronic version of this article is the complete one and can be found online at http 2008 9 8 Rl31 Received 4 June 2008 Revised 24 July 2008 Accepted 2l August 2008 2008 Wegener and Gorbashov licensee BioMed Central Ltd. This is an open access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Background Neuropeptides comprise the most diverse group of neuronal signaling molecules. They often occur as multiple sequence-related copies within single precursors the prepropeptides . These multiple sequence-related copies have not arisen by gene duplication and it is debated whether they are mutually redundant or serve specific functions. The fully sequenced genomes of l2 Drosophila species provide a unique opportunity to study the molecular evolution of neuropeptides. Results We data-mined the 12 Drosophila genomes for homologs of neuropeptide genes identified in Drosophila melanogaster. We then predicted peptide precursors and the neuropeptidome and biochemically identified about half of the predicted peptides by direct mass spectrometric profiling of neuroendocrine tissue in four species covering main phylogenetic lines of Drosophila. We found that all species have an identical neuropeptidome and peptide hormone complement. Calculation of amino acid distances showed that ortholog peptide copies are highly sequence-conserved between .
