Histone chaperone FACT FAcilitates Chromatin Transcription: mechanistic and structural insights

Keda Zhou; Yang Liu; Karolin Luger

doi:10.1016/j.sbi.2020.05.019

Histone chaperone FACT FAcilitates Chromatin Transcription: mechanistic and structural insights

Curr Opin Struct Biol. 2020 Dec:65:26-32. doi: 10.1016/j.sbi.2020.05.019. Epub 2020 Jun 20.

Authors

Keda Zhou¹, Yang Liu², Karolin Luger³

Affiliations

¹ Department of Biochemistry, University of Colorado at Boulder, Boulder, CO 80303, United States.
² Department of Biochemistry, University of Colorado at Boulder, Boulder, CO 80303, United States; Howard Hughes Medical Institute, Chevy Chase, MD 20815, United States.
³ Department of Biochemistry, University of Colorado at Boulder, Boulder, CO 80303, United States; Howard Hughes Medical Institute, Chevy Chase, MD 20815, United States. Electronic address: Karolin.Luger@colorado.edu.

PMID: 32574979
DOI: 10.1016/j.sbi.2020.05.019

Abstract

The histone chaperone FACT (FAcilitates Chromatin Transcription) modulates nucleosome structure during many processes requiring access to chromatinized DNA. Here, we review recent biochemical and structural insight into how FACT acts in both nucleosome assembly and disassembly, to maintain chromatin structure while DNA is being worked on by polymerases.

Publication types

Review

MeSH terms

Chromatin / metabolism
Chromatin Assembly and Disassembly
DNA / metabolism
DNA-Binding Proteins* / chemistry
DNA-Binding Proteins* / metabolism
High Mobility Group Proteins* / chemistry
High Mobility Group Proteins* / metabolism
Histone Chaperones* / chemistry
Histone Chaperones* / metabolism
Histones / metabolism
Humans
Nucleosomes / metabolism
Transcriptional Elongation Factors* / chemistry
Transcriptional Elongation Factors* / metabolism

Substances

Chromatin
DNA-Binding Proteins
High Mobility Group Proteins
Histone Chaperones
Histones
Nucleosomes
SSRP1 protein, human
Transcriptional Elongation Factors
DNA