title: Posttranslational modifications of human histone H3: an update.
abstract: Histone proteins, the fundamental components of chromatin, are highly conserved proteins that present in eukaryotic nuclei. They organize genomic DNA to form nucleosomes, the basic units of chromatin. PTMs of histones play essential roles in many biological processes, such as chromatin condensation, gene expression, cell differentiation, and apoptosis. With the advancement of proteomic technology, a growing number of histone PTMs have been identified, including ADP-ribosylation, biotinylation, citrullination, crotonylation, O-GlcNAcylation, glutathionylation, succinylation, and so on. Because of the fast growing list of these PTMs in just a few years, the functions of these marks are being studied intensively. As histone H3 has the most number of PTMs among the histone members, in this review, we would like to present the overall concepts of the more familiar PTMs as well as discussing all the recently identified yet less well-known PTMs on human histone H3.
authors.affiliation: Laboratory of Cancer Biology and Epigenetics, Department of Cell Biology and Genetics, Shantou University Medical College, Shantou, Guangdong, P. R. China.
authors.forename: Yan-Ming
authors.initials: YM
authors.lastname: Xu
authors.forename: Ji-Ying
authors.initials: JY
authors.lastname: Du
authors.forename: Andy T Y
authors.initials: AT
authors.lastname: Lau
mesh_terms: D001669:Biochemical Phenomena; D006657:Histones / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D013058:Mass Spectrometry; D011499:Protein Processing, Post-Translational
chemical_list: D006657:Histones
keywords: Cell biology; Histone H3; Mass spectrometry; Novel posttranslational modifications; Tandem mass spectrometry