The basic linker of macroH2A stabilizes DNA at the entry/exit site of the nucleosome.
Nucleic Acids Res
; 40(17): 8285-95, 2012 Sep 01.
Article
em En
| MEDLINE
| ID: mdl-22753032
ABSTRACT
MacroH2A is a histone H2A variant that is typically found in heterochromatic regions of the genome. A positively charged linker that connects the histone-fold with the macro-domain was suggested to have DNA-binding properties, and has been shown to promote oligomerization of chromatin fibers. Here we examine the influence of this basic linker on DNA of mononucleosomes. We find that the macro-linker reduces accessibility to extranucleosomal DNA, and appears to increase compaction of the nucleosome. These properties arise from interactions between the H1-like basic linker region and DNA around the entry/exit site, which increases protection of nucleosomal DNA from exonuclease III digestion by â¼10 bp. By stabilizing the wrapping of DNA around the histone core, this basic linker of macroH2A may alter the distribution of nucleosome-associated factors, and potentially contribute to the more compacted nature of heterochromatin.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
DNA
/
Histonas
/
Nucleossomos
Idioma:
En
Ano de publicação:
2012
Tipo de documento:
Article