title: Structural characterization of the histone variant macroH2A.
abstract: macroH2A is an H2A variant with a highly unusual structural organization. It has a C-terminal domain connected to the N-terminal histone domain by a linker. Crystallographic and biochemical studies show that changes in the L1 loop in the histone fold region of macroH2A impact the structure and potentially the function of nucleosomes. The 1.6-A X-ray structure of the nonhistone region reveals an alpha/beta fold which has previously been found in a functionally diverse group of proteins. This region associates with histone deacetylases and affects the acetylation status of nucleosomes containing macroH2A. Thus, the unusual domain structure of macroH2A integrates independent functions that are instrumental in establishing a structurally and functionally unique chromatin domain.
authors.affiliation: Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, 80523-1870, USA.
authors.forename: Srinivas
authors.initials: S
authors.lastname: Chakravarthy
authors.forename: Sampath Kumar Y
authors.initials: SK
authors.lastname: Gundimella
authors.forename: Cecile
authors.initials: C
authors.lastname: Caron
authors.forename: Pierre-Yves
authors.initials: PY
authors.lastname: Perche
authors.forename: John R
authors.initials: JR
authors.lastname: Pehrson
authors.forename: Saadi
authors.initials: S
authors.lastname: Khochbin
authors.forename: Karolin
authors.initials: K
authors.lastname: Luger
mesh_terms: D000107:Acetylation; D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D002522:Chlorocebus aethiops; D002843:Chromatin / Q000378:metabolism; D018360:Crystallography, X-Ray; D006657:Histones / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D014982:Xenopus laevis
chemical_list: D002843:Chromatin; D006657:Histones; C120756:macroH2A histone