Structural highlights
Function
H2A1B_HUMAN
Publication Abstract from PubMed
The human facilitates chromatin transcription (FACT) complex, consisting of Spt16 and SSRP1, is a versatile histone chaperone that can engage free H2A-H2B dimer and H3-H4 tetramer (or dimer), and partially unraveled nucleosome. The C-terminal domain of human Spt16 (hSpt16-CTD) is the decisive element for engaging H2A-H2B dimer and partially unraveled nucleosome. The molecular basis of the H2A-H2B dimer recognitions by hSpt16-CTD is not fully comprehended. Here, we present a high-resolution snapshot of the recognitions of the H2A-H2B dimer by hSpt16-CTD via an acidic intrinsically disordered (AID) segment, and reveal some distinct structural features of hSpt16-CTD as compared to the budding yeast Spt16-CTD.
Structural basis for H2A-H2B recognitions by human Spt16.,Li Y, Huang H Biochem Biophys Res Commun. 2023 Apr 9;651:85-91. doi: , 10.1016/j.bbrc.2023.02.016. Epub 2023 Feb 10. PMID:36801613[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li Y, Huang H. Structural basis for H2A-H2B recognitions by human Spt16. Biochem Biophys Res Commun. 2023 Apr 9;651:85-91. PMID:36801613 doi:10.1016/j.bbrc.2023.02.016
