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Báo cáo y học: " Expansion of the human mitochondrial proteome by intra- and inter-compartmental protein duplication"

Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học Wertheim cung cấp cho các bạn kiến thức về ngành y đề tài: Expansion of the human mitochondrial proteome by intra- and inter-compartmental protein duplication. | Open Access Research Expansion of the human mitochondrial proteome by intra- and inter-compartmental protein duplication Radek Szklarczyk and Martijn A Huynen Address Centre for Molecular and Biomolecular Informatics NCMLS Radboud University Medical Centre 6500 HB Nijmegen The Netherlands. Correspondence Martijn A Huynen. Email huynen@cmbi.ru.nl Published 24 November 2009 Genome Biology 2009 10 RI35 doi 10.1186 gb-2009-I0-II-rI 35 The electronic version of this article is the complete one and can be found online at http genomebiology.com 2009 10 11 R135 2009 Szklarczyk et al. licensee BioMed Central Ltd. This is an open access article distributed under the terms of the Creative Commons Attribution License http creativecommons.org licenses by 2.0 which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Received 9 June 2009 Revised 9 October 2009 Accepted 24 November 2009 Abstract Background Mitochondria are highly complex membrane-enclosed organelles that are essential to the eukaryotic cell. The experimental elucidation of organellar proteomes combined with the sequencing of complete genomes allows us to trace the evolution of the mitochondrial proteome. Results We present a systematic analysis of the evolution of mitochondria via gene duplication in the human lineage. The most common duplications are intra-mitochondrial in which the ancestral gene and the daughter genes encode mitochondrial proteins. These duplications significantly expanded carbohydrate metabolism the protein import machinery and the calcium regulation of mitochondrial activity. The second most prevalent duplication inter-compartmental extended the catalytic as well as the RNA processing repertoire by the novel mitochondrial localization of the protein encoded by one of the daughter genes. Evaluation of the phylogenetic distribution of N-terminal targeting signals suggests a prompt gain of the novel localization after .