RT Journal Article
SR Electronic
T1 The histone chaperone FACT modulates nucleosome structure by tethering its components
JF Life Science Alliance
JO Life Sci. Alliance
FD Life Science Alliance LLC
SP e201800107
DO 10.26508/lsa.201800107
VO 1
IS 4
A1 Tao Wang
A1 Yang Liu
A1 Garrett Edwards
A1 Daniel Krzizike
A1 Hataichanok Scherman
A1 Karolin Luger
YR 2018
UL https://www.life-science-alliance.org/content/1/4/e201800107.abstract
AB Human FAcilitates Chromatin Transcription (hFACT) is a conserved histone chaperone that was originally described as a transcription elongation factor with potential nucleosome assembly functions. Here, we show that FACT has moderate tetrasome assembly activity but facilitates H2A–H2B deposition to form hexasomes and nucleosomes. In the process, FACT tethers components of the nucleosome through interactions with H2A–H2B, resulting in a defined intermediate complex comprising FACT, a histone hexamer, and DNA. Free DNA extending from the tetrasome then competes FACT off H2A–H2B, thereby promoting hexasome and nucleosome formation. Our studies provide mechanistic insight into how FACT may stabilize partial nucleosome structures during transcription or nucleosome assembly, seemingly facilitating both nucleosome disassembly and nucleosome assembly.