Organization and expression of H1 histone and H1 replacement histone genes
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چکیده
منابع مشابه
Nucleotide sequence and expression of a maize H1 histone cDNA.
The first complete amino acid sequence of a H1 histone of a monocotyledonous plant was deduced from a cDNA isolated from a maize library. The encoded H1 protein is 245 amino acid-long and shows the classical tripartite organization of this class of histones. The central globular region of 76 residues shows 60% sequence homology with H1 proteins from dicots but only 20% with the animal H1 protei...
متن کاملReassociation of histone H1 to H1-depleted polynucleosomes.
A new procedure is described for the reassociation of histone H1 to rat liver polynucleosomes selectively depleted of H1 and nonhistone proteins. The fidelity of reconstitution was scrutinized by nuclease digestion and sedimentation studies monitoring the regeneration of structural features which disappear following removal of H1. The results demonstrate that the 166-base pair barrier of digest...
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 کاملReduction of Hox Gene Expression by Histone H1 Depletion
The evolutionarily conserved homeotic (Hox) genes are organized in clusters and expressed collinearly to specify body patterning during embryonic development. Chromatin reorganization and decompaction are intimately connected with Hox gene activation. Linker histone H1 plays a key role in facilitating folding of higher order chromatin structure. Previous studies have shown that deletion of thre...
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: Journal of Cellular Biochemistry
سال: 1994
ISSN: 0730-2312,1097-4644
DOI: 10.1002/jcb.240540409