title: New developments in post-translational modifications and functions of histone H2A variants.
abstract: Structural variability within histone families, such as H2A, can be achieved through 2 primary mechanisms: the expression of histone variants and the incorporation of chemical modifications. The histone H2A family contains several variants in addition to the canonical H2A forms. In this review, recent developments in the study of the heteromorphous variants H2A.X, H2A.Z, and macroH2A will be discussed. Particular focus will be given to the post-translational modifications (PTMs) of these variants, including phosphorylation, ubiquitination, acetylation, and methylation. The combination of the newly identified N- and C-terminal tail PTMs expands the multiplicity of roles that the individual H2A variants can perform. It is of additional interest that analogous sites within these different histone variants can be similarly modified. Whether this is a redundant function or a finely tuned one, designed to meet specific needs, remains to be elucidated.
authors.affiliation: Department of Biochemistry and Microbiology and The Center for Biomedical Research, University of Victoria, Victoria, BCV8W3P6, Canada.
authors.forename: Anita A
authors.initials: AA
authors.lastname: Thambirajah
authors.forename: Andra
authors.initials: A
authors.lastname: Li
authors.forename: Toyotaka
authors.initials: T
authors.lastname: Ishibashi
authors.forename: Juan
authors.initials: J
authors.lastname: Ausió
mesh_terms: D000818:Animals; D042822:Genomic Instability; D006657:Histones / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D020033:Protein Isoforms / Q000737:chemistry / Q000378:metabolism; D011499:Protein Processing, Post-Translational
chemical_list: D006657:Histones; D020033:Protein Isoforms