DNA Accessibility in Nucleosomes
نویسندگان
چکیده
منابع مشابه
Kinetic accessibility of buried DNA sites in nucleosomes.
Using a theoretical model for spontaneous partial DNA unwrapping from histones, we study the transient exposure of protein-binding DNA sites within nucleosomes. We focus on the functional dependence of the rates for site exposure and reburial on the site position, which is measurable experimentally and pertinent to gene regulation. We find the dependence to be roughly described by a random walk...
متن کاملStability of DNA in nucleosomes.
Heats of thermal denaturation of chromatin core particles and core particles with covalently crosslinked histones were measured by differential scanning calorimetry. The additional stabilization of the nucleoprotein complex by crosslinking is not reflected in the transition enthalpy. The contribution of protein denaturation to the total heat was estimated by comparison of core particles with co...
متن کاملPHF1 Tudor and N-terminal domains synergistically target partially unwrapped nucleosomes to increase DNA accessibility
The Tudor domain of human PHF1 recognizes trimethylated lysine 36 on histone H3 (H3K36me3). PHF1 relies on this interaction to regulate PRC2 methyltransferase activity, localize to DNA double strand breaks and mediate nucleosome accessibility. Here, we investigate the impact of the PHF1 N-terminal domain (NTD) on the Tudor domain interaction with the nucleosome. We show that the NTD is partiall...
متن کاملNucleosomes and centromeric DNA packaging.
The eukaryotic chromosome is a conserved structure, with the DNA double-helix wrapping around octamers of histone proteins to form the chromatin, which is further packaged into chromosomes. The centromere defines the kinetochore, the region of spindle microtubule attachment that pulls the two replicated chromatids of each chromosome apart during cell division (Fig. 1), leading to fidelity in tr...
متن کاملKinetics of DNA Unwrapping in Nucleosomes
The eukaryotic genome is organized into complex structures known as nucleosomes, which consist of DNA tightly wrapped around four pairs of proteins called histones. This structure raises questions about the accessibility of the DNA to the proteins that must bind to the DNA for key processes such as transcription and repair. Ingenious experiments in the recent past have suggested that the fluctu...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2010
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2009.12.3314