Nucleosomal core particles lacking one H2A.H2B dimer, (H2A.H2B)1 (H3.H4)2/DNA (146 bp), have been prepared by treatment of nucleosomal cores with dimethylmaleic anhydride, a reversible reagent for protein amino groups. The preparative procedure is simple, produces quantitative conversion of nucleosomal cores into dimer-deficient cores without formation of other subnucleosomal particles, and can be applied to the preparation of different H2A.H2B-deficient mono and oligonucleosomal particles. The structural properties of the dimer-deficient cores and complete nucleosomal cores reconstituted from the deficient particles and H2A.H2B dimers have been studied by DNase I digestion, thermal denaturation and circular dichroism.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/s0006-291x(88)80283-3 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
DNA spontaneously wrapping around a histone core prefers negative supercoiling: A Brownian dynamics study.
PLoS Comput Biol
January 2025
Wenzhou Institute, University of Chinese Academy of Sciences, Wenzhou, Zhejiang, China.
In eukaryotes, DNA achieves a highly compact structure primarily due to its winding around the histone cores. The nature wrapping of DNA around histone core form a 1.7 left-handed superhelical turns, contributing to negative supercoiling in chromatin.
View Article and Find Full Text PDFChromatin conformation, gene transcription, and nucleosome remodeling as an emergent system.
Sci Adv
January 2025
Center for Physical Genomics and Engineering, Northwestern University, Evanston, IL 60208, USA.
In single cells, variably sized nanoscale chromatin structures are observed, but it is unknown whether these form a cohesive framework that regulates RNA transcription. Here, we demonstrate that the human genome is an emergent, self-assembling, reinforcement learning system. Conformationally defined heterogeneous, nanoscopic packing domains form by the interplay of transcription, nucleosome remodeling, and loop extrusion.
View Article and Find Full Text PDFAdvances in the Mechanistic Study of the Control of Oxidative Stress Injury by Modulating HDAC6 Activity.
Cell Biochem Biophys
March 2023
Department of Pathophysiology, Guangdong Medical University, Dongguan, 523808, China.
Oxidative stress is defined as an injury resulting from a disturbance in the dynamic equilibrium of the redox environment due to the overproduction of active/radical oxygen exceeding the antioxidative ability of the body. This is a key step in the development of various diseases. Oxidative stress is modulated by different factors and events, including the modification of histones, which are the cores of nucleosomes.
View Article and Find Full Text PDFThe role of histone deacetylases in embryonic development.
Mol Reprod Dev
January 2023
Department of Biophysics, Manipal School of Life Sciences, Manipal Academy of Higher Education, Manipal, Karnataka, India.
The basic units of chromatin are nucleosomes, that are made up of DNA wrapped around histone cores. Histone lysine residue is a common location for posttranslational modifications, with acetylation being the second most prevalent. Histone acetyltransferases (HATs/KATs) and histone deacetylases (HDACs/KDACs) regulate histone acetylation, which is important in gene expression control.
View Article and Find Full Text PDFA giant virus genome is densely packaged by stable nucleosomes within virions.
Mol Cell
December 2022
Basic Sciences Division, Fred Hutchinson Cancer Research Center, Seattle, WA 98109, USA; Howard Hughes Medical Institute, Chevy Chase, MD, USA. Electronic address:
The two doublet histones of Marseillevirus are distantly related to the four eukaryotic core histones and wrap 121 base pairs of DNA to form remarkably similar nucleosomes. By permeabilizing Marseillevirus virions and performing genome-wide nuclease digestion, chemical cleavage, and mass spectrometry assays, we find that the higher-order organization of Marseillevirus chromatin fundamentally differs from that of eukaryotes. Marseillevirus nucleosomes fully protect DNA within virions as closely abutted 121-bp DNA-wrapped cores without linker DNA or phasing along genes.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!