Li Yue, Huang Hongda
Key Laboratory of Molecular Design for Plant Cell Factory of Guangdong Higher Education Institutes, Department of Chemical Biology & Department of Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen, 518055, China.
Key Laboratory of Molecular Design for Plant Cell Factory of Guangdong Higher Education Institutes, Department of Chemical Biology & Department of Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen, 518055, China.
Biochem Biophys Res Commun. 2023 Apr 9;651:85-91. doi: 10.1016/j.bbrc.2023.02.016. Epub 2023 Feb 10.
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.
由Spt16和SSRP1组成的人类促进染色质转录（FACT）复合物是一种多功能组蛋白伴侣，它可以结合游离的H2A-H2B二聚体和H3-H4四聚体（或二聚体），以及部分解聚的核小体。人类Spt16的C末端结构域（hSpt16-CTD）是结合H2A-H2B二聚体和部分解聚核小体的决定性元件。hSpt16-CTD识别H2A-H2B二聚体的分子基础尚未完全阐明。在此，我们通过一个酸性内在无序（AID）片段展示了hSpt16-CTD识别H2A-H2B二聚体的高分辨率快照，并揭示了与芽殖酵母Spt16-CTD相比hSpt16-CTD的一些独特结构特征。
