Structural characterization of the histone variant macroH2A.
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.
Chakravarthy
Srinivas
S
Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, 80523-1870, USA.
Gundimella
Sampath Kumar Y
SK
Caron
Cecile
C
Perche
Pierre-Yves
PY
Pehrson
John R
JR
Khochbin
Saadi
S
Luger
Karolin
K
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
D002843:Chromatin; D006657:Histones; C120756:macroH2A histone