ArticleNucleic acids research2018
Oligomerization of Drosophila Nucleoplasmin-Like Protein is required for its centromere localization.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 14 citations in OpenAlex.
- Molecular conflicts disrupting centromere maintenance contribute to Xenopus hybrid inviability.Current biology : CB · 2022Article
- Stimulated emission depletion microscopy with a single depletion laser using five fluorochromes and fluorescence lifetime phasor separation.Scientific reports · 2022Article
- Comprehensive genomic survey, structural classification and expression analysis of CBMC plant biology · 2021Article
- The Integrity of the HMR complex is necessary for centromeric binding and reproductive isolation in Drosophila.PLoS genetics · 2021Article
- Mutual dependency between lncRNA LETN and protein NPM1 in controlling the nucleolar structure and functions sustaining cell proliferation.Cell research · 2021Article
- A multi-layered structure of the interphase chromocenter revealed by proximity-based biotinylation.Nucleic acids research · 2020Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
The evolutionarily conserved nucleoplasmin family of histone chaperones has two paralogues in Drosophila, named Nucleoplasmin-Like Protein (NLP) and Nucleophosmin (NPH). NLP localizes to the centromere, yet molecular underpinnings of this localization are unknown. Moreover, similar to homologues in other organisms, NLP forms a pentamer in vitro, but the biological significance of its oligomerization has not been explored. Here, we characterize the oligomers formed by NLP and NPH in vivo and find that oligomerization of NLP is required for its localization at the centromere. We can further show that oligomerization-deficient NLP is unable to bind the centromeric protein Hybrid Male Rescue (HMR), which in turn is required for targeting the NLP oligomer to the centromere. Finally, using super-resolution microscopy we find that NLP and HMR largely co-localize in domains that are immediately adjacent to, yet distinct from centromere domains defined by the centromeric histone dCENP-A.
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Registered trials
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