Rxivist logo

The histone chaperone FACT modulates nucleosome structure by tethering its components

By Tao Wang, Yang Liu, Garrett Edwards, Daniel Krzizike, Hataichanok Scherman, Karolin Luger

Posted 27 Apr 2018
bioRxiv DOI: 10.1101/309708 (published DOI: 10.26508/lsa.201800107)

Human FACT (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 facilitates tetrasome assembly and 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 comprised of 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 nucleosome disassembly and nucleosome assembly.

Download data

  • Downloaded 644 times
  • Download rankings, all-time:
    • Site-wide: 34,338
    • In biochemistry: 843
  • Year to date:
    • Site-wide: 57,893
  • Since beginning of last month:
    • Site-wide: 80,852

Altmetric data

Downloads over time

Distribution of downloads per paper, site-wide


Sign up for the Rxivist weekly newsletter! (Click here for more details.)