ArticleScientific reports2015
Crystal Structure of Human SSRP1 Middle Domain Reveals a Role in DNA Binding.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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Who cites it
24 citing papers in PubMed, 35 citations in OpenAlex.
- Proximal proteomics analysis reveals DNA polymerase δ subunit 3 is a new MCM2 binding partner and promotes parental histones inheritance in mammalian cells.Cell death and differentiation · 2026Article
- FACT depletion results in a temporal cascade of chromatin disruption preceding transcriptional collapse in stem cells.bioRxiv : the preprint server for biology · 2026Article
- Insights into FACT in Cancers with Targeted Therapeutic Implications.Molecular and cellular biology · 2026Review
- A Novel ceRNA Axis LOC121818100/Novel-miR-400/SSRP1 Regulated Muscle Growth and Injury Repair in Sheep.Journal of cachexia, sarcopenia and muscle · 2025Article
- The FAcilitates Chromatin Transcription complex regulates the ratio of glycolysis to oxidative phosphorylation in neural stem cells.Journal of molecular cell biology · 2024Article
- Review
- Opposing Roles of FACT for Euchromatin and Heterochromatin in Yeast.Biomolecules · 2023Review
- The Histone Chaperone Network Is Highly Conserved inInternational journal of molecular sciences · 2023Article
- SSRP1 affects the growth and apoptosis of gastric cancer cells through AKT pathway.Journal of medical biochemistry · 2022Article
- A Panel of E2F Target Gene Signature Predicting the Prognosis of Hepatocellular Carcinoma.Frontiers in genetics · 2022Article
- SSRP1 Is a Prognostic Biomarker Correlated with CD8BioMed research international · 2021Article
- The Histone Chaperone FACT Induces Cas9 Multi-turnover Behavior and Modifies Genome Manipulation in Human Cells.Molecular cell · 2020Article
- SSRP1-mediated histone H1 eviction promotes replication origin assembly and accelerated development.Nature communications · 2020Article
- Article
- Unresolved Complexity in the Gene Regulatory Network Underlying EMT.Frontiers in oncology · 2020Review
- 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
- SSRP1 silencing inhibits the proliferation and malignancy of human glioma cells via the MAPK signaling pathway.Oncology reports · 2017Article
- Fly Fishing for Histones: Catch and Release by Histone Chaperone Intrinsically Disordered Regions and Acidic Stretches.Journal of molecular biology · 2017Review
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SSRP1 is a subunit of the FACT complex, an important histone chaperone required for transcriptional regulation, DNA replication and damage repair. SSRP1 also plays important roles in transcriptional regulation independent of Spt16 and interacts with other proteins. Here, we report the crystal structure of the middle domain of SSRP1. It consists of tandem pleckstrin homology (PH) domains. These domains differ from the typical PH domain in that PH1 domain has an extra conserved βαβ topology. SSRP1 contains the well-characterized DNA-binding HMG-1 domain. Our studies revealed that SSRP1-M can also participate in DNA binding, and that this binding involves one positively charged patch on the surface of the structure. In addition, SSRP1-M did not bind to histones, which was assessed through pull-down assays. This aspect makes the protein different from other related proteins adopting the double PH domain structure. Our studies facilitate the understanding of SSRP1 and provide insights into the molecular mechanisms of interaction with DNA and histones of the FACT complex.
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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.