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.

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

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.

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.

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 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 tandem SH2 domains of Spt6 use novel mechanisms to bind unexpected phosphorylated serine and threonine residues in the RNA polymerase II linker to recruit Spt6 to sites of transcription and maintain repressive chromatin.

Analysis of aging yeast cells using the in-vivo roGFP2-based probe reveals redox-dependent heterogeneity, reflected in a bi-modal distribution of the oxidation status, differential growth and replication, as well as distinct proteomic and transcriptomic profiles.