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.
Ura
K
K
Laboratory of Molecular Embryology, NICHD, National Institutes of Health, Bethesda, Maryland 20892.
Wolffe
A P
AP
Hayes
J J
JJ
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