The association of histones with specific chaperone complexes is important for their folding,
oligomerization, post-translational modification, nuclear import, stability, assembly and …

Nucleosomes compact and organize genetic material on a structural level. However, they
also alter local chromatin accessibility through changes in their position, through the …

A multitude of histone chaperones are required to support histones from their biosynthesis
until DNA deposition. They cooperate through the formation of histone co-chaperone …

DNA damage triggers chromatin remodeling by mechanisms that are poorly understood.
The oncogene and chromatin remodeler ALC1/CHD1L massively decompacts chromatin in …

Nucleosomes represent the fundamental repeating unit of eukaryotic DNA, and comprise
eight core histones around which DNA is wrapped in nearly two superhelical turns. Histones …

One of the first events to occur upon DNA damage is the local opening of the compact
chromatin architecture, facilitating access of repair proteins to DNA lesions. This early …

Histone chaperones regulate all aspects of histone metabolism. NASP is a major histone
chaperone for H3–H4 dimers critical for preventing histone degradation. Here, we identify …

Newly synthesised histones are thought to dimerise in the cytosol and undergo nuclear
import in complex with histone chaperones. Here, we provide evidence that human H3. 1 …

Core histones package chromosomal DNA and regulate genomic transactions, with their
nuclear import and deposition involving importin-β proteins and a dedicated repertoire of …

Centromeres define the chromosomal position where kinetochores form to link the
chromosome to microtubules during mitosis and meiosis. Centromere identity is determined …