ArticleScientific reports2017
Basic surface features of nuclear FKBPs facilitate chromatin binding.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 27 citations in OpenAlex.
- Chromatin localization of nucleophosmin organizes ribosome biogenesis.Molecular cell · 2022Article
- Intrabronchial application of extracellular histones shows no proinflammatory effects in swine in a translational pilot study.BMC research notes · 2021Article
- FKBP25 participates in DNA double-strand break repair.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2020Article
- Histone Chaperone Paralogs Have Redundant, Cooperative, and Divergent Functions in Yeast.Genetics · 2019Article
- The prolyl isomerase FKBP25 regulates microtubule polymerization impacting cell cycle progression and genomic stability.Nucleic acids research · 2018Article
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Authors and funding
11 authors at 4 institutions in 4 countries.
Funding
Abstract
The nucleoplasmin family of histone chaperones is identified by a pentamer-forming domain and multiple acidic tracts that mediate histone binding and chaperone activity. Within this family, a novel domain organization was recently discovered that consists of an N-terminal nucleoplasmin-like (NPL) domain and a C-terminal FKBP peptidyl-proline isomerase domain. Saccharomyces cerevisiae Fpr4 is one such protein. Here we report that in addition to its known histone prolyl isomerase activities, the Fpr4 FKBP domain binds to nucleosomes and nucleosome arrays in vitro. This ability is mediated by a collection of basic patches that enable the enzyme to stably associate with linker DNA. The interaction of the Fpr4 FKBP with recombinant chromatin complexes condenses nucleosome arrays independently of its catalytic activity. Based on phylogenetic comparisons we propose that the chromatin binding ability of 'basic' FKBPs is shared amongst related orthologues present in fungi, plants, and insects. Thus, a subclass of FKBP prolyl isomerase enzymes is recruited to linker regions of chromatin.
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