In an unusual complex that is not dissociated by RanGTP alone, Importin-9 sequesters the H2A-H2B core from promiscuous interactions.

After DNA replication, nucleosomes are assembled by two histone chaperone complexes each bound to an H3-H4 histone dimer, suggesting the feasibility for a semi-conservative mode of epigenome inheritance.

Biophysical and biochemical approaches reveal new insights into the architecture of CAF-1 and the unique mechanism by which CAF-1 tetramerizes histones H3/H4.

Histone, PCNA, and DNA binding are essential for CAF-1 functions in preventing DNA damage during DNA replication in Schizosaccharomyces pombe, while its C-terminal domain specifies distinct cellular processes.

Histone H3 can translocate to the nucleus as a monomer through a pathway governed by importin-5 and transfers to the histone chaperone NASP, having implications in the folding of H3-H4 dimers and, therefore, the kinetics of genome packaging during replication.

The Chd1 motor protein performs two functionally distinct ATP-dependent activities, nucleosome assembly and chromatin remodeling, to generate periodic arrays of nucleosomes.

The CAF1 complex binds single histone H3-H4 dimers, and two such complexes associate with extended DNA elements to ensure the deposition of H3-H4 tetramers, the first step in the assembly of nucleosomes.

The histone chaperone FACT and the deubiquitinating enzyme Ubp10 act in concert to remove ubiquitin from histone H2B in nucleosomes, and likely coordinate nucleosome assembly during DNA replication and transcription.

Internally tagged, functional Cse4/CENP-A/CenH3 histone variant is exclusively centromeric and stable through the budding yeast cell cycle after replacement in S phase.

The human genome is unpackaged to allow DNA breaks to be joined back together, and then repackaged into chromosomes afterwards.