ArticleJournal of molecular biology2015
The pentameric nucleoplasmin fold is present in Drosophila FKBP39 and a large number of chromatin-related proteins.
Article in Journal of molecular biology, 2015. 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, 34 citations in OpenAlex.
- Genome-Wide Analysis of Tea FK506-Binding Proteins (FKBPs) Reveals ThatInternational journal of molecular sciences · 2025Article
- Identification, characterization and spatiotemporal expression analysis of the FKBP family genes in Locusta migratoria.Scientific reports · 2023Article
- HD-tuin proteins, the ugly ducklings of histone deacetylases.The Plant cell · 2022Article
- Plant-specific HDT family histone deacetylases are nucleoplasmins.The Plant cell · 2022Article
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- AtFKBP53: a chimeric histone chaperone with functional nucleoplasmin and PPIase domains.Nucleic acids research · 2020Article
- FKBP25 participates in DNA double-strand break repair.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2020Article
- Structure-function relationship of H2A-H2B specific plant histone chaperones.Cell stress & chaperones · 2020Review
- Histone Chaperone Paralogs Have Redundant, Cooperative, and Divergent Functions in Yeast.Genetics · 2019Article
- Comparative analysis of FKBP family protein: evaluation, structure, and function in mammals and Drosophila melanogaster.BMC developmental biology · 2018Review
- Canonical and Noncanonical Actions of Arabidopsis Histone Deacetylases in Ribosomal RNA Processing.The Plant cell · 2018Article
- Fly Fishing for Histones: Catch and Release by Histone Chaperone Intrinsically Disordered Regions and Acidic Stretches.Journal of molecular biology · 2017Review
- Basic surface features of nuclear FKBPs facilitate chromatin binding.Scientific reports · 2017Article
- Nucleoplasmin-like domain of FKBP39 from Drosophila melanogaster forms a tetramer with partly disordered tentacle-like C-terminal segments.Scientific reports · 2017Article
- The composition and organization of Drosophila heterochromatin are heterogeneous and dynamic.eLife · 2016Article
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 3 countries.
Funding
Abstract
Nucleoplasmin is a histone chaperone that consists of a pentameric N-terminal domain and an unstructured C-terminal tail. The pentameric core domain, a doughnut-like structure with a central pore, is only found in the nucleoplasmin family. Here, we report the first structure of a nucleoplasmin-like domain (NPL) from the unrelated Drosophila protein, FKBP39, and we present evidence that this protein associates with chromatin. Furthermore, we show that two other chromatin proteins, Arabidopsis thaliana histone deacetylase type 2 (HD2) and Saccharomyces cerevisiae Fpr4, share the NPL fold and form pentamers, or a dimer of pentamers in the case of HD2. Thus, we propose a new family of proteins that share the pentameric nucleoplasmin-like NPL domain and are found in protists, fungi, plants and animals.
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