Temperature and osmotic stress dependence of the thermodynamics for binding linker histone H1 0 , Its carboxyl domain (H1 0 -C) or globular domain (H1 0 -G) to B-DNA
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چکیده
منابع مشابه
Temperature and osmotic stress dependence of the thermodynamics for binding linker histone H10, Its carboxyl domain (H10-C) or globular domain (H10-G) to B-DNA
Linker histones (H1) are the basic proteins in higher eukaryotes that are responsible for the final condensation of chromatin. In contrast to the nucleosome core histone proteins, the role of H1 in compacting DNA is not clearly understood. In this study ITC was used to measure the binding constant, enthalpy change, and binding site size for the interactions of H10, or its C-terminal (H10-C) and...
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Antibodies to the folding domain (residues 22-100) of histone H5 were elicited in rabbits. Analysis of the specificity of these antibodies by enzyme-linked immunoassay and by diazobenzyloxymethyl cellulose transfer techniques revealed that the antibody cross-reacts strongly with intact H5 and histones H1(0)a and H1(0)b purified from ox liver but not with the four core calf thymus, or with high ...
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In most eukaryotes, two classes of histone genes are present: i) replication-dependent, the expression of which is restricted to the S phase of cell cycle and ii) replicationindependent or basal genes, expressed at low but quite constant level throughout the cell cycle (for review see ref. 1). Histone genes in the first class are characterized by lack of introns; corresponding mRNAs are not pol...
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We previously documented condensation of the H1 CTD consistent with adoption of a defined structure upon nucleosome binding using a bulk FRET assay, supporting proposals that the CTD behaves as an intrinsically disordered domain. In the present study, by determining the distances between two different pairs of sites in the C-terminal domain of full length H1 by FRET, we confirm that nucleosome ...
متن کاملBinding 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 ...
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ژورنال
عنوان ژورنال: Biochemistry and Biophysics Reports
سال: 2017
ISSN: 2405-5808
DOI: 10.1016/j.bbrep.2017.09.009