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Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học quốc tế cung cấp cho các bạn kiến thức về ngành y đề tài: A scale of functional divergence for yeast duplicated genes revealed from analysis of the protein-protein interaction network. | Research Open Access A scale of functional divergence for yeast duplicated genes revealed from analysis of the protein-protein interaction network Ana is Baudot Bernard Jacq and Christine Brun Address Laboratoire de Génétique et Physiologie du Développement IBDM CNRS INSERM Université de la Méditerranée Parc Scientifique de Luminy Case 907 13288 Marseille Cedex 9 France. Correspondence Christine Brun. E-mail brun@ibdm.univ-mrs.fr Published 15 September 2004 Genome Biology 2004 5 R76 The electronic version of this article is the complete one and can be found online at http genomebiology.com 2004 5 10 R76 Received 24 March 2004 Revised 11 June 2004 Accepted 2 August 2004 2004 Baudot 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. Abstract Background Studying the evolution of the function of duplicated genes usually implies an estimation of the extent of functional conservation divergence between duplicates from comparison of actual sequences. This only reveals the possible molecular function of genes without taking into account their cellular function s . We took into consideration this latter dimension of gene function to approach the functional evolution of duplicated genes by analyzing the proteinprotein interaction network in which their products are involved. For this we derived a functional classification of the proteins using PRODISTIN a bioinformatics method allowing comparison of protein function. Our work focused on the duplicated yeast genes remnants of an ancient wholegenome duplication. Results Starting from 4 143 interactions we analyzed 41 duplicated protein pairs with the PRODISTIN method. We showed that duplicated pairs behaved differently in the classification with respect to their interactors. The .
