Vps75 is a histone chaperone that has been historically characterized as homodimer by X-
ray crystallography. In this study, we present a crystal structure containing two related …

The histone chaperone Vps75 presents the remarkable property of stimulating the Rtt109-
dependent acetylation of several histone H3 lysine residues within (H3-H4) 2 tetramers. To …

Histone acetylation and nucleosome remodeling regulate DNA damage repair, replication
and transcription. Rtt109, a recently discovered histone acetyltransferase (HAT) from …

In this issue of Cell, English et al.(2006) present the first crystal structure of a histone
chaperone (Asf1) bound to histones (the H3/H4 heterodimer). The structure provides …

Histone chaperones physically interact with histones to direct proper assembly and
disassembly of nucleosomes regulating diverse nuclear processes such as DNA replication …

Most histone acetyltransferases (HATs) function as multisubunit complexes in which
accessory proteins regulate substrate specificity and catalytic efficiency. Rtt109 is a …

Eukaryotic gene expression is regulated by histone deposition onto and eviction from
nucleosomes, which are mediated by several chromatin-modulating factors. Among them …

Asf1 is a histone chaperone that favors histone H3/H4 assembly and disassembly. We
solved the structure of the conserved domain of human ASF1A in complex with the C …

Acetylation of histone H3 on lysine 56 occurs during mitotic and meiotic S phase in fungal
species. This acetylation blocks a direct electrostatic interaction between histone H3 and …

Acetylation of Saccharomyces cerevisiae histone H3 on K56 by the histone
acetyltransferase (HAT) Rtt109 is important for repairing replication-associated lesions …