The histone variant H2A. Z is involved in several processes such as transcriptional control,
DNA repair, regulation of centromeric heterochromatin and, not surprisingly, is implicated in …

When fully extended, one copy of the three billion base pair human genome reaches a
length of over two meters. Yet, it must be packaged into the nucleus of a cell with an average …

The NuA4/TIP60 acetyltransferase complex is a key regulator of genome expression and
stability. Here we identified MBTD1 as a stable subunit of the complex, and we reveal that …

Deoxyribonucleic acid in eukaryotes wraps around the histone octamer to form
nucleosomes, the fundamental unit of chromatin. The N termini of histone H4 interact with …

Histone acetyltransferases (HATs) assemble into multisubunit complexes in order to target
distinct lysine residues on nucleosomal histones. Here, we characterize native HAT …

The ATP-dependent chromatin-remodeling complex SWR1 exchanges a variant histone
H2A. Z/H2B dimer for a canonical H2A/H2B dimer at nucleosomes flanking histone-depleted …

Commonly used methods for determining protein structure, including X-ray crystallography
and single-particle reconstruction, often provide a single and unique three-dimensional (3D) …

The NuA4/TIP60 acetyltransferase complex is required for gene regulation, DNA repair and
cell cycle progression. The limited structural information impeded understanding of …

NuA4 catalyzes the acetylation of nucleosomes at histone H4, which is a well-established
epigenetic event, controlling many genomic processes in Saccharomyces cerevisiae. Here …

The NuA4 protein complex acetylates histones H4 and H2A to activate both transcription
and DNA repair. We report the 3.1-Å resolution cryo-electron microscopy structure of the …