ArticleMolecular reproduction and development2018
Combined functions of two RRMs in Dead-end1 mimic helicase activity to promote nanos1 translation in the germline.
Article in Molecular reproduction and development, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Germ plasm dynamics during oogenesis and early embryonic development in Xenopus and zebrafish.Molecular reproduction and development · 2024Review
- High throughput isolation of RNA from single-cells within an intact tissue for spatial and temporal sequencing a reality.PloS one · 2023Article
- Biochemical and subcellular characterization of a squid hnRNPA/B-like protein 2 in osmotic stress activated cells reflects molecular properties conserved in this protein family.Molecular biology reports · 2022Article
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- The Role of DND1 in Cancers.Cancers · 2021Review
- Human DND1-RRM2 forms a non-canonical domain swapped dimer.Protein science : a publication of the Protein Society · 2021Article
- MC4R mutant mice develop ovarian teratomas.Scientific reports · 2021Article
- The RNA-binding protein DND1 acts sequentially as a negative regulator of pluripotency and a positive regulator of epigenetic modifiers required for germ cell reprogramming.Development (Cambridge, England) · 2019Article
- Novel functions of the ubiquitin-independent proteasome system in regulatingDevelopment (Cambridge, England) · 2019Article
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Authors and funding
7 authors at 3 institutions in 4 countries.
Funding
Abstract
Dead-end1 (Dnd1) expression is restricted to the vertebrate germline where it is believed to activate translation of messenger RNAs (mRNAs) required to protect and promote that unique lineage. Nanos1 is one such germline mRNA whose translation is blocked by a secondary mRNA structure within the open reading frame (ORF). Dnd1 contains a canonical RNA recognition motif (RRM1) in its N-terminus but also contains a less conserved RRM2. Here we provide a mechanistic picture of the nanos1 mRNA-Dnd1 interaction in the Xenopus germline. We show that RRM1, but not RRM2, is required for binding nanos1. Similar to the zebrafish homolog, Xenopus Dnd1 possesses ATPase activity. Surprisingly, this activity appears to be within the RRM2, different from the C-terminal region where it is found in zebrafish. More importantly, we show that RRM2 is required for nanos1 translation and germline survival. Further, Dnd1 functions as a homodimer and binds nanos1 mRNA just downstream of the secondary structure required for nanos1 repression. We propose a model in which the RRM1 is required to bind nanos1 mRNA while the RRM2 is required to promote translation through the action of ATPase. Dnd1 appears to use RRMs to mimic the function of helicases.
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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 Socratic graph.