Core histone acetylation does not block linker histone binding to a nucleosome including a Xenopus borealis 5 S rRNA gene.
We demonstrate that acetylation of core histone tails does not significantly impair the ability of linker histones to bind preferentially and asymmetrically to a defined sequence mononucleosome core reconstituted in vitro. Thus a simple inhibition mechanism cannot explain models whereby acetylation is causal for the observed reduction in the linker histone content in chromatin. Other models to explain this correlation are discussed.
Laboratory of Molecular Embryology, NICHD, National Institutes of Health, Bethesda, Maryland 20892.
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K
Ura
A P
AP
Wolffe
J J
JJ
Hayes
D000107:Acetylation; D000818:Animals; D002474:Cell-Free System; D004275:DNA, Ribosomal / Q000378:metabolism*; D006367:HeLa Cells; D006657:Histones / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D009707:Nucleosomes / Q000378:metabolism*; D011485:Protein Binding; D012341:RNA, Ribosomal, 5S / Q000235:genetics; D014981:Xenopus
D004275:DNA, Ribosomal; D006657:Histones; D009707:Nucleosomes; D012341:RNA, Ribosomal, 5S