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Functional involvement of Tudor and dPRMT5 in the piRNA processing pathway in Drosophila germlines
Open accessAbstract
In Drosophila, the PIWI proteins, Aubergine (Aub), AGO3, and Piwi are expressed in germlines and function in silencing transposons by associating with PIWI-interacting RNAs (piRNAs). Recent studies show that PIWI proteins contain symmetric dimethyl-arginines (sDMAs) and that dPRMT5/Capsuleen/DART5 is the modifying enzyme. Here, we show that Tudor (Tud), one of Tud domain-containing proteins, associates with Aub and AGO3, specifically through their sDMA modifications and that these three proteins form heteromeric complexes. piRNA precursor-like molecules are detected in these complexes. The expression levels of Aub and AGO3, along with their degree of sDMA modification, were not changed by tud mutations. However, the population of transposon-derived piRNAs associated with Aub and AGO3 was altered by tud mutations, whereas the total amounts of small RNAs on Aub and AGO3 was increased. Loss of dprmt5 did not change the stability of Aub, but impaired its association with Tud and lowered piRNA association with Aub. Thus, in germline cells, piRNAs are quality-controlled by dPRMT5 that modifies PIWI proteins, in tight association with Tud.
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Metadata
- Authors
- Nishida, K. M., Okada, T. N., Kawamura, T., Mituyama, T., Kawamura, Y., Inagaki, S., Huang, H., Chen, D., Kodama, T., Siomi, H., & Siomi, M. C.
- Affiliations
- Keio University (JP)
- Research Center for Advanced Science and Technology, The University of Tokyo (JP)
- Chinese Academy of Sciences (CN)
- Corresponding author
- Siomi, Mikiko C
- ORCID
- Venue
- The EMBO Journal
- Published
- 2009-12-03
- Volume
- 28
- Issue
- 24
- Pages
- 3820-3831
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC2797066
- OpenAlex
- W2136921460
- Cited by
- 197
- References
- 45
- Citations by year
- 2026: 2 · 2025: 8 · 2024: 9 · 2023: 6 · 2022: 7 · 2021: 8 · 2020: 11 · 2019: 10 · 2018: 16 · 2017: 11 · 2016: 11 · 2015: 13 · 2014: 11 · 2013: 16 · 2012: 20
- FWCI
- 23.47
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ministry of Education, Culture, Sports, Science and Technology (CREST)
- University of Tokushima
- Japan Society for the Promotion of Science (CREST)
- Japan Science and Technology Agency (CREST)
- Core Research for Evolutional Science and Technology
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Chromosomal and Genetic Variations
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Interference and Gene Delivery
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- Tudor domain, piRNA, PIWI proteins, eggplant, AGO3, Piwi, symmetric dimethylarginine, arginine methylation, transposon silencing, germline, Drosophila
- MeSH terms
- Amino Acid Sequence, Animals, Arginine, Chromatography, Liquid, Drosophila melanogaster, Gene Expression Regulation, Molecular Sequence Data, Mutation, Protein-Arginine N-Methyltransferases, Protein Methyltransferases, Mass Spectrometry, Sequence Homology, Amino Acid, Membrane Transport Proteins, Drosophila Proteins, Databases, Protein, RNA Interference
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