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 …

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 …

Histone chaperones have been implicated in nucleosome assembly and disassembly as
well as histone modification. ASF1 is a highly conserved histone H3/H4 chaperone that …

Summary Anti-silencing function 1 (Asf1) is a highly conserved chaperone of histones H3/H4
that assembles or disassembles chromatin during transcription, replication, and repair. The …

The recent two years have led to the realization that histone chaperones contribute to the
delicate balance between nucleosome assembly and re-assembly during transcription, and …

Histone chaperones are proteins that interact with histones to regulate the thermodynamic
process of nucleosome assembly. sNASP and ASF1 are conserved histone chaperones that …

Some three decades have passed since the discovery of nucleosomes in 1974 and the first
isolation of a histone chaperone in 1978. While various types of histone chaperones have …

The packaging of eukaryotic DNA into chromatin presents a formidable barrier to enzymes
that must access the DNA template–such as RNA and DNA polymerase-while at the same …

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

Abstract Human HIRA, ASF1a, ASF1b and CAF-1 are evolutionally conserved histone
chaperones that form multiple functionally distinct chromatin-assembly complexes, with roles …