Evidence for the nucleosome-disruption process regulated by phosphorylation of 120 kDa protein complex in Drosophila embryo cell-free system.
Using cell-free system derived from Drosophila embryos, we found evidence for a regulated nucleosome disruption process, which depends on the phosphorylation status of 120 kDa protein (complex). Dephosphorylation enables the remodeling activity to destabilize nucleosomes, which assume a more accessible structure, possessing increased DNase I sensitivity and high conformational flexibility of DNA; remodeling was more efficient on highly acetylated chromatin templates. This phosphorylation-regulated nucleosome destabilization, acting synergistically with histone acetylation, is discussed as a possible mechanism to provide regulated disrupt of histone-DNA interaction.
Institute of Developmental Biology, Moscow, Russian Federation. wkrajewski@hotmail.com
Wladyslaw A
WA
Krajewski
D000107:Acetylation; D000818:Animals; D002474:Cell-Free System; D002843:Chromatin / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism; D004330:Drosophila / Q000196:embryology / Q000378:metabolism*; D029721:Drosophila Proteins / Q000378:metabolism*; D004625:Embryo, Nonmammalian / Q000378:metabolism; D006657:Histones / Q000378:metabolism; D009707:Nucleosomes / Q000378:metabolism*; D010766:Phosphorylation
D002843:Chromatin; D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; D006657:Histones; D009707:Nucleosomes