ArticleThe Journal of biological chemistry2009
Phosphorylated intrinsically disordered region of FACT masks its nucleosomal DNA binding elements.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 62 citations in OpenAlex.
- MYC drives left-handed Z-DNA formation to shape gene expression.Nature communications · 2025Article
- Versatile roles of disordered transcription factor effector domains in transcriptional regulation.The FEBS journal · 2025Review
- Interactions with multiple inner kinetochore proteins determine mitotic localization of FACT.The Journal of cell biology · 2025Article
- The Histone Chaperone Network Is Highly Conserved inInternational journal of molecular sciences · 2023Article
- Dynamic structures of intrinsically disordered proteins related to the general transcription factor TFIIH, nucleosomes, and histone chaperones.Biophysical reviews · 2022Review
- Phosphorylation of the FACT histone chaperone subunit SPT16 affects chromatin at RNA polymerase II transcriptional start sites in Arabidopsis.Nucleic acids research · 2022Article
- The Current Status of SSRP1 in Cancer: Tribulation and Road Ahead.Journal of healthcare engineering · 2022Review
- Genome-Wide Association Analysis of Anoxia Tolerance inG3 (Bethesda, Md.) · 2019Article
- Structural visualization of key steps in nucleosome reorganization by human FACT.Scientific reports · 2019Article
- Histone Chaperone FACT and Curaxins: Effects on Genome Structure and Function.Journal of cancer metastasis and treatment · 2019Article
- Transcription Promotes the Interaction of the FAcilitates Chromatin Transactions (FACT) Complex with Nucleosomes inGenetics · 2018Article
- Mechanism of FACT removal from transcribed genes by anticancer drugs curaxins.Science advances · 2018Article
- Structure and function of the histone chaperone FACT - Resolving FACTual issues.Biochimica et biophysica acta. Gene regulatory mechanisms · 2018Review
- Structure-specific recognition protein-1 (SSRP1) is an elongated homodimer that binds histones.The Journal of biological chemistry · 2018Article
- Functional roles of the DNA-binding HMGB domain in the histone chaperone FACT in nucleosome reorganization.The Journal of biological chemistry · 2018Article
- FACT is a sensor of DNA torsional stress in eukaryotic cells.Nucleic acids research · 2017Article
- The Structure-Specific Recognition Protein 1 Associates with Lens Epithelium-Derived Growth Factor Proteins and Modulates HIV-1 Replication.Journal of molecular biology · 2016Article
- Integrated molecular mechanism directing nucleosome reorganization by human FACT.Genes & development · 2016Article
- Crystal Structure of Human SSRP1 Middle Domain Reveals a Role in DNA Binding.Scientific reports · 2015Article
- A large-scale in vivo RNAi screen to identify genes involved in Notch-mediated follicle cell differentiation and cell cycle switches.Scientific reports · 2015Article
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
FACT is a heterodimer of SPT16 and SSRP1, which each contain several conserved regions in the primary structure. The interaction of FACT with nucleosomes induces chromatin remodeling through the combinatorial action of its distinct functional protein regions. However, there is little mechanistic insight into how these regions cooperatively contribute to FACT functions, particularly regarding the recognition of nucleosomal DNA. Here, we report the identification of novel phosphorylation sites of Drosophila melanogaster FACT (dFACT) expressed in Sf9 cells. These sites are densely concentrated in the acidic intrinsically disordered (ID) region of the SSRP1 subunit and control nucleosomal DNA binding by dFACT. This region and the adjacent segment of the HMG domain form weak electrostatic intramolecular interactions, which is reinforced by the phosphorylation, thereby blocking DNA binding competitively. Importantly, this control mechanism appears to support rapid chromatin transactions during early embryogenesis through the dephosphorylation of some sites in the maternally transmitted dSSRP1.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.