ArticleCommunications biology2019
Structural and biochemical analyses of the nuclear pore complex component ELYS identify residues responsible for nucleosome binding.
Article in Communications biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 19 citations in OpenAlex.
- Structural basis of nucleosome remodeling by Cockayne syndrome B homologue Komagataella phaffii Rad26.Nature communications · 2026Article
- Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025Review
- Article
- AHCTF1 Functions as an Oncogenic Factor and Promotes Tumor Progression in Hepatocellular Carcinoma.Digestive diseases and sciences · 2025Article
- Nucleoporin Elys attaches peripheral chromatin to the nuclear pores in interphase nuclei.Communications biology · 2024Article
- Interactions of Chromatin with the Nuclear Lamina and Nuclear Pore Complexes.International journal of molecular sciences · 2023Review
- Article
- Structure and Function of the Nuclear Pore Complex.Cold Spring Harbor perspectives in biology · 2022Review
- Architecture of the cytoplasmic face of the nuclear pore.Science (New York, N.Y.) · 2022Article
- Time Resolved-Fluorescence Resonance Energy Transfer platform for quantitative nucleosome binding and footprinting.Protein science : a publication of the Protein Society · 2022Article
- Multivalent DNA and nucleosome acidic patch interactions specify VRK1 mitotic localization and activity.Nucleic acids research · 2022Article
- Review
- The Role of Nucleoporin Elys in Nuclear Pore Complex Assembly and Regulation of Genome Architecture.International journal of molecular sciences · 2020Review
- Comprehensive nucleosome interactome screen establishes fundamental principles of nucleosome binding.Nucleic acids research · 2020Article
- Nucleosome binding by the pioneer transcription factor OCT4.Scientific reports · 2020Article
- Chromatin Compaction Multiscale Modeling: A Complex Synergy Between Theory, Simulation, and Experiment.Frontiers in molecular biosciences · 2020Review
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nuclear pore complex embedded within the nuclear envelope is the essential architecture for trafficking macromolecules, such as proteins and RNAs, between the cytoplasm and nucleus. The nuclear pore complex assembly occurs on chromatin in the post-mitotic phase of the cell cycle. ELYS (MEL-28/AHCTF1) binds to the nucleosome, which is the basic chromatin unit, and promotes assembly of the complex around the chromosomes in cells. Here we show that the Arg-Arg-Lys (RRK) stretch of the C-terminal ELYS region plays an essential role in the nucleosome binding. The cryo-EM structure and the crosslinking mass spectrometry reveal that the ELYS C-terminal region directly binds to the acidic patch of the nucleosome. These results provide mechanistic insight into the ELYS-nucleosome interaction, which promotes the post-mitotic nuclear pore complex formation around chromosomes in cells.
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