Results 11 to 20 of about 141,257 (371)

Multiple structures of RNA polymerase II isolated from human nuclei by ChIP-CryoEM analysis [PDF]

open access: yesNature Communications
RNA polymerase II (RNAPII) is a central transcription enzyme that exists as multiple forms with or without accessory factors, and transcribes the genomic DNA packaged in chromatin.
Tomoya Kujirai   +12 more
doaj   +2 more sources

The size of the nucleosome [PDF]

open access: yes, 2011
The structural origin of the size of the 11 nm nucleosomal disc is addressed. On the nanometer length-scale the organization of DNA as chromatin in the chromosomes involves a coiling of DNA around the histone core of the nucleosome. We suggest that the size of the nucleosome core particle is dictated by the fulfillment of two criteria: One is ...
Bohr, Jakob, Olsen, Kasper
openaire   +4 more sources

Structure of nucleosome-bound human PBAF complex

open access: yesbioRxiv, 2022
BAF and PBAF are mammalian SWI/SNF family chromatin remodeling complexes that possess multiple histone/DNA-binding subunits and create nucleosome-depleted/free regions for transcription activation. Despite structural studies of nucleosome-bound human BAF
Li Wang   +8 more
semanticscholar   +1 more source

Structural basis of nucleosome disassembly and reassembly by RNAPII elongation complex with FACT

open access: yesScience, 2022
During gene transcription, RNA polymerase II (RNAPII) traverses nucleosomes in chromatin, but the mechanism has remained elusive. Using cryo–electron microscopy, we obtained structures of the RNAPII elongation complex (EC) passing through a nucleosome in
H. Ehara   +4 more
semanticscholar   +1 more source

Predicting human nucleosome occupancy from primary sequence. [PDF]

open access: yesPLoS Computational Biology, 2008
Nucleosomes are the fundamental repeating unit of chromatin and comprise the structural building blocks of the living eukaryotic genome. Micrococcal nuclease (MNase) has long been used to delineate nucleosomal organization.
Shobhit Gupta   +5 more
doaj   +1 more source

Structural basis of nucleosome retention during transcription elongation

open access: yesScience, 2022
In eukaryotes, RNA polymerase (Pol) II transcribes chromatin and must move past nucleosomes, often resulting in nucleosome displacement. How Pol II unwraps the DNA from nucleosomes to allow transcription and how DNA rewraps to retain nucleosomes has been
Martin Filipovski   +3 more
semanticscholar   +1 more source

Structural Transition of the Nucleosome during Transcription Elongation

open access: yesCells, 2023
In eukaryotes, genomic DNA is tightly wrapped in chromatin. The nucleosome is a basic unit of chromatin, but acts as a barrier to transcription. To overcome this impediment, the RNA polymerase II elongation complex disassembles the nucleosome during ...
Tomoya Kujirai   +3 more
doaj   +1 more source

Histone H1 binding to nucleosome arrays depends on linker DNA length and trajectory

open access: yesNature Structural & Molecular Biology, 2022
Throughout the genome, nucleosomes often form regular arrays that differ in nucleosome repeat length (NRL), occupancy of linker histone H1 and transcriptional activity. Here, we report cryo-EM structures of human H1-containing tetranucleosome arrays with
Marco Dombrowski   +4 more
semanticscholar   +1 more source

Nucleosome Switches [PDF]

open access: yesPhysical Review Letters, 2008
We present a statistical-mechanical analysis of the positioning of nucleosomes along one of the chromosomes of yeast DNA as a function of the strength of the binding potential and of the chemical potential of the nucleosomes. We find a significant density of two-level nucleosome switching regions where, as a function of the chemical potential, the ...
David J. Schwab   +3 more
openaire   +4 more sources

H3.3-H4 tetramer splitting events feature cell-type specific enhancers. [PDF]

open access: yesPLoS Genetics, 2013
Previously, we reported that little canonical (H3.1-H4)(2) tetramers split to form "hybrid" tetramers consisted of old and new H3.1-H(4) dimers, but approximately 10% of (H3.3-H4)2 tetramers split during each cell cycle.
Chang Huang   +7 more
doaj   +1 more source

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