title: Post-translational modifications of linker histone H1 variants in mammals.
abstract: The covalent modifications of the linker histone H1 and the core histones are thought to play an important role in the control of chromatin functioning. Histone H1 variants from K562 cell line (hH1), mouse (mH1) and calf (cH1) thymi were studied by matrix-activated laser desorption/ionization fourier transform ion cyclotron resonance mass-spectroscopy (MALDI-FT-ICR-MS). The proteomics analysis revealed novel post-translational modifications of the histone H1, such as meK34-mH1.4, meK35-cH1.1, meK35-mH1.1, meK75-hH1.2, meK75-hH1.3, acK26-hH1.4, acK26-hH1.3 and acK17-hH1.1. The comparison of the hH1, mH1 and cH1 proteins has demonstrated that the types and positions of the post-translational modifications of the globular domains of the H1.2-H1.4 variants are very conservative. However, the post-translational modifications of the N- and C-terminal tails of H1.2, H1.3 and H1.4 are different. The differences of post-translational modifications in the N- and C-terminal tails of H1.2, H1.3 and H1.4 likely lead to the differences in DNA-H1 and H1-protein interactions.
authors.affiliation: Institute of Cytology of the Russian Academy of Sciences, St Petersburg, Russia. Saint Petersburg State University, Saint Petersburg, Russia. Author to whom any correspondence should be addressed. The authors made equal contribution to preparation of the manuscript.
authors.forename: T Yu
authors.initials: TY
authors.lastname: Starkova
authors.forename: A M
authors.initials: AM
authors.lastname: Polyanichko
authors.forename: T O
authors.initials: TO
authors.lastname: Artamonova
authors.forename: M A
authors.initials: MA
authors.lastname: Khodorkovskii
authors.forename: E I
authors.initials: EI
authors.lastname: Kostyleva
authors.forename: E V
authors.initials: EV
authors.lastname: Chikhirzhina
authors.forename: A N
authors.initials: AN
authors.lastname: Tomilin
mesh_terms: D000107:Acetylation; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002460:Cell Line; D004247:DNA / Q000378:metabolism; D006657:Histones / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008745:Methylation; D051379:Mice; D010766:Phosphorylation; D000072417:Protein Domains; D011499:Protein Processing, Post-Translational; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D006657:Histones; D004247:DNA