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XB-ART-1487
Mol Cell Biol 2005 Sep 01;2517:7616-24. doi: 10.1128/MCB.25.17.7616-7624.2005.
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Structural characterization of the histone variant macroH2A.

Chakravarthy S , Gundimella SK , Caron C , Perche PY , Pehrson JR , Khochbin S , Luger K .


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.

PubMed ID: 16107708
PMC ID: PMC1190287
Article link: Mol Cell Biol


Species referenced: Xenopus laevis
Genes referenced: h2ac21 macroh2a1

References [+] :
Abbott, Characterization of the stability and folding of H2A.Z chromatin particles: implications for transcriptional activation. 2001, Pubmed