Structural rearrangements of the histone octamer translocate DNA [PDF]
Nature Communications, 2018 Nucleosomes are dynamic and can move along DNA in an uncatalyzed manner but little is known about the mechanisms of histone octamer translocation. Here the authors present cryo-EM structures of nucleosomes in differently organized histone octamer and DNA
Silvija Bilokapic +2 more
doaj +10 more sources
Role of the histone tails in histone octamer transfer. [PDF]
Nucleic Acids Res, 2023 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.
Lorch Y, Kornberg RD, Maier-Davis B.
europepmc +6 more sources
Retroviral integration into nucleosomes through DNA looping and sliding along the histone octamer [PDF]
Nature Communications, 2019 Retroviral integrases catalyze the insertion of viral DNA into the host cell DNA and can use nucleosomes as substrates for integration. Here the authors present the 3.9 Å cryo-EM structure of prototype foamy virus integrase after strand transfer into ...
Marcus D. Wilson +8 more
doaj +7 more sources
Rapid reconstitution of ubiquitinated nucleosome using a non-denatured histone octamer ubiquitylation approach [PDF]
Cell & BioscienceBackground Histone ubiquitination modification is emerging as a critical epigenetic mechanism involved in a range of biological processes. In vitro reconstitution of ubiquitinated nucleosomes is pivotal for elucidating the influence of histone ...
Weijie Li +19 more
doaj +5 more sources
Histone octamer rearranges to adapt to DNA unwrapping. [PDF]
Nat Struct Mol Biol, 2018 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.
Bilokapic S, Strauss M, Halic M.
europepmc +9 more sources
SMARCAD1 is an ATP-dependent histone octamer exchange factor with de novo nucleosome assembly activity. [PDF]
Sci Adv, 2021 An ATP-dependent remodeler engages nucleosomes in a unique manner.
Markert J, Zhou K, Luger K.
europepmc +3 more sources
Histone Octamer Instability under Single Molecule Experiment Conditions [PDF]
Journal of Biological Chemistry, 2005 We have studied the sample concentration-dependent and external stress-dependent stability of native and reconstituted nucleosomal arrays. Whereas upon stretching a single chromatin fiber in a solution of very low chromatin concentration the statistical distribution of DNA length released upon nucleosome unfolding shows only one population centered ...
Cyrille Claudet +4 more
semanticscholar +8 more sources
Cancer-associated histone mutation H2BG53D disrupts DNA-histone octamer interaction and promotes oncogenic phenotypes. [PDF]
Signal Transduct Target Ther, 2020 Publication details: Wan, Y. C. E., Leung, T. C. S., Ding, D., Sun, X., Liu, J., Zhu, L., Kang, T. Z. E., Yang, D., Zhang, Y., Zhang, J., Qian, C., Huen, M. S. Y., Li, Q., Chow, M. Z.
Wan YCE +19 more
europepmc +6 more sources
Distortion of histone octamer core promotes nucleosome mobilization by a chromatin remodeler. [PDF]
Science, 2017 Sinha KK, Gross JD, Narlikar GJ.
europepmc +4 more sources
Basic helix-loop-helix pioneer factors interact with the histone octamer to invade nucleosomes and generate nucleosome depleted regions [PDF]
bioRxiv, 2022 Nucleosomes drastically limit transcription factor (TF) occupancy, while pioneer transcription factors (PFs) somehow circumvent this nucleosome barrier. In this study, we compare nucleosome binding of two conserved S.
Benjamin Donovan +7 more
openalex +2 more sources