Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học Critical Care giúp cho các bạn có thêm kiến thức về ngành y học đề tài: Post-translational modifications of histones H3 and H4 associated with the histone methyltransferases Suv39h1 and G9a. | Open Access Method Post-translational modifications of histones H3 and H4 associated with the histone methyltransferases Suv39h1 and G9a Philippe Robin Lauriane Fritsch Ophélie Philipot Fedor SvinarchuV and Slimane Ait-Si-Ali Addresses Centre National de la Recherche Scientifique CNRS FRE 2944 Institut André Lwoff rue Guy Moquet Villejuif F-94801 France Université Paris-Sud Villejuif F-94801 France. Centre National de la Recherche Scientifique CNRS FRE 3018 GENETHON bis rue de l Internationale Evry F-91002 France Université d Evry Evry F-91002 France. Correspondence Slimane Ait-Si-Ali. Email aitsiali@ Published 20 December 2007 Biology 2007 8 R270 doi gb-2007-8- l2-r270 The electronic version of this article is the complete one and can be found online at http 2007 8 12 R270 Received 2 October 2007 Revised 6 December 2007 Accepted 20 December 2007 2008 Robin et al. 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 Specific combinations of post-translational modifications of histones alter chromatin structure facilitating gene transcription or silencing. Here we have investigated the histone code associated with the histone methyltransferases Suv39h1 and G9a by combining double immunopurification and mass spectrometry. Our results confirm the previously reported histone modifications associated with Suv39h1 and G9a. Moreover this method allowed us to demonstrate for the first time an association of acetylated histones with the repressor proteins Suv39h1 and G9a. Background The amino-terminal tails of nucleosomal histones protrude from the DNA and are subject to covalent modifications. These modifications include lysine acetylation lysine and arginine methylation serine and threonine
