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Báo cáo khoa học: Post-translational modifications of the linker histone variants and their association with cell mechanisms

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In recent years, a considerable amount of research has been focused on estab-lishing the epigenetic mechanisms associated with DNA and the core histones. This effort is driven by the fact that epigenetics is intimately involved with genomics in a whole range of molecular processes. However, there is now a consensus that the epigenetics of the linker histones are just as important. | ỊFEBS Journal REVIEW ARTICLE Post-translational modifications of the linker histone variants and their association with cell mechanisms Christopher Wood1 Ambrosius Snijders2 James Williamson2 Colin Reynolds1 John Baldwin3 and Mark Dickman2 1 Schoolof Pharmacy and Biomolecular Sciences LiverpoolJohn Moores University UK 2 Department of Chemicaland Process Engineering University of Sheffield UK 3 STFC Daresbury Laboratory Warrington UK Keywords abundance acid extraction cancer cell cycle disease linker histone MS post-translationalmodification PTM PTM function Correspondence C. M. Wood Schoolof Pharmacy and Biomolecular Sciences Liverpool John Moores University Liverpool UK Fax 44 0 51 298 2624 Tel 44 0 51 231 2565 E-mail c.m.wood@ljmu.ac.uk Received 10 December 2008 revised 23 March 2009 accepted 30 April 2009 doi 10.1111 j.1742-4658.2009.07079.x In recent years a considerable amount of research has been focused on establishing the epigenetic mechanisms associated with DNA and the core histones. This effort is driven by the fact that epigenetics is intimately involved with genomics in a whole range of molecular processes. However there is now a consensus that the epigenetics of the linker histones are just as important. The result of that consensus is that the post-translational modifications PTMs for most of the linker histone variants in human and mouse have now been established by a number of experimental techniques foremost of which is mass spectrometry MS . MS was also used by our group to establish the PTMs of the linker histone variants in chicken erythrocytes. Although it is now known which types of PTM occur at particular locations on the linker histone variants there is still a large gap in the knowledge of how this data relates to function. The focus of this review is an analysis of the PTM data for the linker histones from several species but with an emphasis on human mouse and chicken. Our analysis reveals that certain PTMs can be clearly correlated .

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