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The basic linker of macroH2A stabilizes DNA at the entry/exit site of the nucleosome.

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 ?10?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.

SUBMITTER: Chakravarthy S

PROVIDER: S-EPMC3458575 | biostudies-other | 2012 Sep

REPOSITORIES: biostudies-other

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The basic linker of macroH2A stabilizes DNA at the entry/exit site of the nucleosome.

Chakravarthy Srinivas S Patel Ashok A Bowman Gregory D GD

Nucleic acids research 20120629 17

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 nucleosom ...[more]

PMID: 22753032

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