Results 1 to 10 of about 50 (49)
Role of the histone tails in histone octamer transfer
Nucleic Acids Research, 2023 Abstract The exceptionally high positive charge of the histones, concentrated in the N- and C-terminal tails, is believed to contribute to the stability of the nucleosome by neutralizing the negative charge of the nucleosomal DNA. We find, on the contrary, that the high positive charge contributes to instability, performing an essential ...
Yahli Lorch +2 more
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Isolation of the yeast histone octamer. [PDF]
Proceedings of the National Academy of Sciences, 1994 Procedures for the extraction and purification of the yeast histone octamer are described. Either mechanical disruption, yielding chromatin fragments, or spheroplast formation with subsequent nuclear isolation was employed. A hexahistidine tag was inserted in the N-terminal region of histone H2B, permitting resolution of the histone octamer from high ...
Roger D. Kornberg, Yahli Lorch
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A NMR study of mobility in the histone octamer [PDF]
FEBS Letters, 1990 The histone octamer from chicken erythrocytes was studied in 2 M NaCI using 500 mHz 1H NMR spectroscopy. We compared the spectrum of control octamers with that of octamers isolated from trypsinized nucleosome core particles. We observe that the sharp resonances found in the spectrum of the native octamer disappear completely after trypsinization ...
E. Morton Bradbury +5 more
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Structural rearrangements of the histone octamer translocate DNA [PDF]
Nature Communications, 2018 AbstractNucleosomes, the basic unit of chromatin, package and regulate expression of eukaryotic genomes. Nucleosomes are highly dynamic and are remodeled with the help of ATP-dependent remodeling factors. Yet, the mechanism of DNA translocation around the histone octamer is poorly understood.
Silvija Bilokapic +2 more
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Folding of single‐stranded DNA on the histone octamer [PDF]
FEBS Letters, 1985 A complex between the single‐stranded DNA of the bacteriophage M13 and the histone octamer was analyzed by electron microscopy, low‐angle X‐ray diffraction and nuclease analysis. The morphology and the diffraction pattern of the complex strongly resemble those of the nucleosome.
Caffarelli E, Leoni L, Savino M
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An octamer of histones in chromatin and free in solution. [PDF]
Proceedings of the National Academy of Sciences, 1975 Crosslinking with dimethyl suberimidate reveals a chain of histone octamers in chromatin. The octamer can be isolated free in solution at high ionic strength and pH. The identification of dimers formed by crosslinking reveals two or more contacts of each histone with others within the octamer.
Roger D. Kornberg, Jean O. Thomas
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Points of contact between histone H1 and the histone octamer. [PDF]
Proceedings of the National Academy of Sciences, 1980 The topography of the interaction between histone H1 and the histone octamer has been investigated. Bovine thymus nuclei or enzymatically fragmented chromatin were treated 1-ethyl-3(3-dimethylaminopropyl)carbodiimide, which catalyzes the formation of covalent bonds between residues of proteins in electrostatic contact.
John M. Wiseman +2 more
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Histone octamer rearranges to adapt to DNA unwrapping [PDF]
Nature Structural & Molecular Biology, 2017 Nucleosomes, the basic units of chromatin, package and regulate expression of eukaryotic genomes. Although the structure of the intact nucleosome is well characterized, little is known about structures of partially unwrapped, transient intermediates.
Silvija Bilokapic +2 more
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Histone Octamer Transfer by a Chromatin-Remodeling Complex [PDF]
Cell, 1999 RSC, an abundant, essential chromatin-remodeling complex related to SWI/SNF complex, catalyzes the transfer of a histone octamer from a nucleosome core particle to naked DNA. The newly formed octamer-DNA complex is identical with a nucleosome in all respects. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. The mechanism
Roger D. Kornberg +2 more
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Chaperoning of the histone octamer by the acidic domain of DNA repair factor APLF [PDF]
Science Advances, 2021 Nucleosome assembly requires the coordinated deposition of histone complexes H3-H4 and H2A-H2B to form a histone octamer on DNA. In the current paradigm, specific histone chaperones guide the deposition of first H3-H4 and then H2A-H2B. Here, we show that the acidic domain of DNA repair factor APLF (APLF AD ) can ...
Corbeski, Ivan +14 more
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