ArticleActa crystallographica. Section F, Structural biology communications2016
Structure of the human histone chaperone FACT Spt16 N-terminal domain.
Article in Acta crystallographica. Section F, Structural biology communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- SUPT16H-associated neurodevelopmental disorder and neurocristopathy: genetic and phenotypic spectrum.Human molecular genetics · 2026Article
- Abo1 ATPase facilitates the dissociation of FACT from chromatin.Nucleic acids research · 2025Article
- Facilitates Chromatin Transcription in Breast and Other Cancers.Advances in experimental medicine and biology · 2024Review
- The N-terminus of Spt16 anchors FACT to MCM2-7 for parental histone recycling.Nucleic acids research · 2023Article
- Mechanism of curaxin-dependent nucleosome unfolding by FACT.Frontiers in molecular biosciences · 2022Article
- Structure-function relationship of H2A-H2B specific plant histone chaperones.Cell stress & chaperones · 2020Review
- Structure-specific recognition protein-1 (SSRP1) is an elongated homodimer that binds histones.The Journal of biological chemistry · 2018Article
- Charged residues on the side of the nucleosome contribute to normal Spt16-gene interactions in budding yeast.Epigenetics · 2018Article
- Fly Fishing for Histones: Catch and Release by Histone Chaperone Intrinsically Disordered Regions and Acidic Stretches.Journal of molecular biology · 2017Review
- Review
- Regulation of chromatin structure and function: insights into the histone chaperone FACT.Cell cycle (Georgetown, Tex.)Review
- Evidence that dissociation of Spt16 from transcribed genes is partially dependent on RNA Polymerase II termination.TranscriptionArticle
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
The histone chaperone FACT plays an important role in facilitating nucleosome assembly and disassembly during transcription. FACT is a heterodimeric complex consisting of Spt16 and SSRP1. The N-terminal domain of Spt16 resembles an inactive aminopeptidase. How this domain contributes to the histone chaperone activity of FACT remains elusive. Here, the crystal structure of the N-terminal domain (NTD) of human Spt16 is reported at a resolution of 1.84 Å. The structure adopts an aminopeptidase-like fold similar to those of the Saccharomyces cerevisiae and Schizosaccharomyces pombe Spt16 NTDs. Isothermal titration calorimetry analyses show that human Spt16 NTD binds histones H3/H4 with low-micromolar affinity, suggesting that Spt16 NTD may contribute to histone binding in the FACT complex. Surface-residue conservation and electrostatic analysis reveal a conserved acidic patch that may be involved in histone binding.
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