Interaction of the intrinsically-disordered linker histone C-terminal tail with DNA.

DOI

In cells, the genome needs to be tightly packaged in the nucleus as "chromatin" while still allowing access to the cellular machinery responsible for gene expression. The first level of packaging involves the "core histone” proteins, which form spools around which two turns of DNA are wrapped, a series of which gives rise to an array resembling "beads on a string". This is further condensed by "linker histone" proteins, one of which binds to each spool, arranging them into a thicker fibre. The precise way in which this is accomplished is, despite decades of research, still a hotly debated topic since linker histones have long tails that do not have a static defined 3D structure even when bound to the linker DNA that they are directly responsible for condensing, thus conventional diffraction-based methods fail. We aim to use SANS for this important piece of the chromatin structure puzzle.

Identifier
DOI https://doi.org/10.5286/ISIS.E.87813643
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/87813643
Provenance
Creator Dr Katherine Stott; Dr Matthew Watson; Dr Najet Mahmoudi
Publisher ISIS Neutron and Muon Source
Publication Year 2020
Rights CC-BY Attribution 4.0 International; https://creativecommons.org/licenses/by/4.0/
OpenAccess true
Contact isisdata(at)stfc.ac.uk
Representation
Resource Type Dataset
Discipline Biology; Biomaterials; Engineering Sciences; Life Sciences; Materials Science; Materials Science and Engineering
Temporal Coverage Begin 2017-10-09T08:00:00Z
Temporal Coverage End 2017-10-10T20:12:35Z