Structural basis for H2A–H2B recognitions by human Spt16
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.
First ; Corresponding
|ESI Research Field|
BIOLOGY & BIOCHEMISTRY
Cited Times [WOS]:0
|Document Type||Journal Article|
|Department||Department of Biology|
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
|First Author Affilication||Department of Biology; School of Life Sciences; Department Of Chemical Biology And Quantitative Biology|
|Corresponding Author Affilication||Department of Biology; School of Life Sciences; Department Of Chemical Biology And Quantitative Biology|
|First Author's First Affilication||Department of Biology; School of Life Sciences; Department Of Chemical Biology And Quantitative Biology|
Li，Yue,Huang，Hongda. Structural basis for H2A–H2B recognitions by human Spt16[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,2023,651:85-91.
Li，Yue,&Huang，Hongda.(2023).Structural basis for H2A–H2B recognitions by human Spt16.BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,651,85-91.
Li，Yue,et al."Structural basis for H2A–H2B recognitions by human Spt16".BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 651(2023):85-91.
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