منابع مشابه
Binding of phosphorylated histone H1 to DNA.
A chromatin associated protein kinase was used to add 3 moles of phosphate to seryl side chains of 1 mole of histone H1. The DNA binding properties of this in vitro phosphorylated H1 were compared with those of unmodified H1. Considerably more radioactive superhelical DNA was retained on nitrocellulose filters at 20mM-40mM NaCl by phosphorylated H1 than by unmodified H1. However, zone velocity ...
متن کاملCondensation of polynucleosome by histone H1 binding.
The cooperative binding of histone H1 to polynucleosome was studied quantitatively. The equilibrium and kinetic data were satisfactorily described in terms of the large ligand model. The binding constant K and the cooperativity parameter q showed remarkable salt effects: K = 7.5 X 10(7) M-1 and q = 1.3 X 10(4) at 0.2 M NaCl, pH 7.5 and 20 degrees C. This considerably strong cooperativity reveal...
متن کاملThe anticancer agent ellipticine unwinds DNA by intercalative binding in an orientation parallel to base pairs.
Ellipticine is a natural plant product that has been found to be a powerful anticancer drug. Although still unclear, its mechanism of action is considered to be mainly based on DNA intercalation and/or the inhibition of topoisomerase II. Many experimental data suggest an intercalation based on stacking interactions along the major base-pair axis, but alternative binding modes have been proposed...
متن کاملHistone H1 binding is inhibited by histone variant H3.3.
Linker histones are involved in the formation of higher-order chromatin structure and the regulation of specific genes, yet it remains unclear what their principal binding determinants are. We generated a genome-wide high-resolution binding map for linker histone H1 in Drosophila cells, using DamID. H1 binds at similar levels across much of the genome, both in classic euchromatin and heterochro...
متن کاملHigh-affinity binding sites for histone H1 in plasmid DNA.
The interaction of histone H1 isolated from chicken erythrocytes with restriction fragments from plasmids pBR322 and pUC19 was studied by gel electrophoresis. Certain restriction fragments exhibited unusually high affinity for the histone, forming high molecular mass complexes at protein to DNA ratios at which the other fragments did not show evidence for binding. The highly preferred fragments...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1996
ISSN: 0021-9258
DOI: 10.1074/jbc.271.51.32580