ArticleBiology direct2010
OST-HTH: a novel predicted RNA-binding domain.
Article in Biology direct, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 79 citations in OpenAlex.
- Structural basis for recognition of diverse localizing mRNAs by Egl-BicD.Nature structural & molecular biology · 2026Article
- LOTUS-domain proteins activate Vasa to drive germ granule assembly.bioRxiv : the preprint server for biology · 2026Article
- Molecular insights into the Drosophila piRNA pathway via systematic ReLo protein interaction screening and structure prediction.Nucleic acids research · 2025Article
- The RRM domain-containing protein Rbp3 interacts with ribosomes and the 3' ends of mRNAs encoding photosynthesis proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- piRNA processing within non-membrane structures is governed by constituent proteins and their functional motifs.The FEBS journal · 2025Review
- The LOTUS domain of Oskar promotes localisation of both protein and mRNA components ofbioRxiv : the preprint server for biology · 2025Article
- Regulators of male and female sexual development are critical for the transmission of a malaria parasite.Cell host & microbe · 2023Article
- The Caenorhabditis elegans TDRD5/7-like protein, LOTR-1, interacts with the helicase ZNFX-1 to balance epigenetic signals in the germline.PLoS genetics · 2022Article
- TDRD5 Is Required for Spermatogenesis and Oogenesis inInsects · 2022Article
- Highly Overexpressed AtC3H18 Impairs MicrogametogenesisFrontiers in plant science · 2022Article
- RNA-binding proteins and post-transcriptional regulation in lens biology and cataract: Mediating spatiotemporal expression of key factors that control the cell cycle, transcription, cytoskeleton and transparency.Experimental eye research · 2022Review
- Evolution of a Cytoplasmic Determinant: Evidence for the Biochemical Basis of Functional Evolution of the Novel Germ Line Regulator Oskar.Molecular biology and evolution · 2021Article
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- Early germline differentiation in bivalves: TDRD7 as a candidate investigational unit for Ruditapes philippinarum germ granule assembly.Histochemistry and cell biology · 2021Article
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- Genome-Wide Analysis of Differentially Expressed miRNAs and Their Associated Regulatory Networks in Lenses Deficient for the Congenital Cataract-Linked Tudor Domain Containing Protein TDRD7.Frontiers in cell and developmental biology · 2021Article
- Patterning the Drosophila embryo: A paradigm for RNA-based developmental genetic regulation.Wiley interdisciplinary reviews. RNA · 2020Review
- Phosphoglycerate kinase: structural aspects and functions, with special emphasis on the enzyme from Kinetoplastea.Open biology · 2020Review
- LOTUS domain is a novel class of G-rich and G-quadruplex RNA binding domain.Nucleic acids research · 2020Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundThe mechanism by which the arthropod Oskar and vertebrate TDRD5/TDRD7 proteins nucleate or organize structurally related ribonucleoprotein (RNP) complexes, the polar granule and nuage, is poorly understood. Using sequence profile searches we identify a novel domain in these proteins that is widely conserved across eukaryotes and bacteria.
resultsUsing contextual information from domain architectures, sequence-structure superpositions and available functional information we predict that this domain is likely to adopt the winged helix-turn-helix fold and bind RNA with a potential specificity for dsRNA. We show that in eukaryotes this domain is often combined in the same polypeptide with protein-protein- or lipid- interaction domains that might play a role in anchoring these proteins to specific cytoskeletal structures.
conclusionsThus, proteins with this domain might have a key role in the recognition and localization of dsRNA, including miRNAs, rasiRNAs and piRNAs hybridized to their targets. In other cases, this domain is fused to ubiquitin-binding, E3 ligase and ubiquitin-like domains indicating a previously under-appreciated role for ubiquitination in regulating the assembly and stability of nuage-like RNP complexes. Both bacteria and eukaryotes encode a conserved family of proteins that combines this predicted RNA-binding domain with a previously uncharacterized domain (DUF88). We present evidence that it is an RNAse belonging to the superfamily that includes the 5'->3' nucleases, PIN and NYN domains and might be recruited to degrade certain RNAs.
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Registered trials
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 OpenQuestion graph.