Post-translational modifications of the linker histone variants and their association with cell mechanisms.
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 with specific functions of the linker histones in particular cell types, and that unique PTM patterns exist for different cell types.
Wood
Christopher
C
School of Pharmacy and Biomolecular Sciences, Liverpool John Moores University, UK. c.m.wood@ljmu.ac.uk
Snijders
Ambrosius
A
Williamson
James
J
Reynolds
Colin
C
Baldwin
John
J
Dickman
Mark
M
D000818:Animals; D002468:Cell Physiological Phenomena; D044127:Epigenesis, Genetic; D014644:Genetic Variation; D006657:Histones / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D013045:Species Specificity
D006657:Histones