ArticleProceedings of the National Academy of Sciences of the United States of America2017
Structural basis for arginine methylation-independent recognition of PIWIL1 by TDRD2.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed, 35 citations in OpenAlex.
- Molecular insights into the Drosophila piRNA pathway via systematic ReLo protein interaction screening and structure prediction.Nucleic acids research · 2025Article
- R-Methylation in Plants: A Key Regulator of Plant Development and Response to the Environment.International journal of molecular sciences · 2024Review
- The functions and mechanisms of piRNAs in mediating mammalian spermatogenesis and their applications in reproductive medicine.Cellular and molecular life sciences : CMLS · 2024Review
- Arabidopsis AGO1 N-terminal extension acts as an essential hub for PRMT5 interaction and post-translational modifications.Nucleic acids research · 2024Article
- MIWI N-terminal arginines orchestrate generation of functional pachytene piRNAs and spermiogenesis.Nucleic acids research · 2024Article
- piRNA loading triggers MIWI translocation from the intermitochondrial cement to chromatoid body during mouse spermatogenesis.Nature communications · 2024Article
- MIWI arginines orchestrate generation of functional pachytene piRNAs and spermiogenesis.bioRxiv : the preprint server for biology · 2024Article
- MIWI N-terminal RG motif promotes efficient pachytene piRNA production and spermatogenesis independent of LINE1 transposon silencing.PLoS genetics · 2023Article
- Two RNA binding proteins, ADAD2 and RNF17, interact to form a heterogeneous population of novel meiotic germ cell granules with developmentally dependent organelle association.PLoS genetics · 2023Article
- Effectors and effects of arginine methylation.Biochemical Society transactions · 2023Article
- TDRD5 Is Required for Spermatogenesis and Oogenesis inInsects · 2022Article
- Binding of guide piRNA triggers methylation of the unstructured N-terminal region of Aub leading to assembly of the piRNA amplification complex.Nature communications · 2021Article
- Knockout Gene-Based Evidence for PIWI-Interacting RNA Pathway in Mammals.Frontiers in cell and developmental biology · 2021Review
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- Mitochondrial membrane-based initial separation of MIWI and MILI functions during pachytene piRNA biogenesis.Nucleic acids research · 2019Article
- The physiological and pathological biophysics of phase separation and gelation of RNA binding proteins in amyotrophic lateral sclerosis and fronto-temporal lobar degeneration.Brain research · 2018Review
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- Structural insights into the sequence-specific recognition of Piwi byProceedings of the National Academy of Sciences of the United States of America · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 4 institutions in 3 countries.
Funding
Abstract
The P-element-induced wimpy testis (PIWI)-interacting RNA (piRNA) pathway plays a central role in transposon silencing and genome protection in the animal germline. A family of Tudor domain proteins regulates the piRNA pathway through direct Tudor domain-PIWI interactions. Tudor domains are known to fulfill this function by binding to methylated PIWI proteins in an arginine methylation-dependent manner. Here, we report a mechanism of methylation-independent Tudor domain-PIWI interaction. Unlike most other Tudor domains, the extended Tudor domain of mammalian Tudor domain-containing protein 2 (TDRD2) preferentially recognizes an unmethylated arginine-rich sequence from PIWI-like protein 1 (PIWIL1). Structural studies reveal an unexpected Tudor domain-binding mode for the PIWIL1 sequence in which the interface of Tudor and staphylococcal nuclease domains is primarily responsible for PIWIL1 peptide recognition. Mutations disrupting the TDRD2-PIWIL1 interaction compromise piRNA maturation via 3'-end trimming in vitro. Our work presented here reveals the molecular divergence of the interactions between different Tudor domain proteins and PIWI proteins.
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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.