Structural characterization of the histone variant macroH2A. Journal Article uri icon

Overview

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.

publication date

  • September 1, 2005

Full Author List

  • Chakravarthy S; Gundimella SKY; Caron C; Perche P-Y; Pehrson JR; Khochbin S; Luger K

Other Profiles

Additional Document Info

start page

  • 7616

end page

  • 7624

volume

  • 25

issue

  • 17