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Arabidopsis TRM5 encodes a nuclear-localised bifunctional tRNA guanine and inosine-N1-methyltransferase that is important for growth
Open accessPreprint — published as 10.1371/journal.pone.0225064 · Paper page
Abstract
Modified nucleosides in tRNAs are critical for protein translation. N 1 -methylguanosine-37 and N 1 -methylinosine-37 in tRNAs, both located at the 3’-adjacent to the anticodon, are formed by Trm5 and here we describe Arabidopsis thaliana AtTrm5 (At3g56120) as a Trm5 ortholog. We show that AtTrm5 complements the yeast trm5 mutant, and in vitro methylates tRNA guanosine-37 to produce N 1 -methylguanosine (m 1 G). We also show in vitro that AtTRM5 methylates tRNA inosine-37 to produce N 1 -methylinosine (m 1 I) and in Attrm5 mutant plants, we show a reduction of both N 1 -methylguanosine and N 1 -methylinosine. We also show that AtTRM5 is localized to the nucleus in plant cells. Attrm5 mutant plants have overall slower growth as observed by slower leaf initiation rate, delayed flowering and reduced primary root length. In Attrm5 mutants, mRNAs of flowering time genes are less abundant and correlated with delayed flowering. Finally, proteomics data show that photosynthetic protein abundance is affected in mutant plants. Our findings highlight the bifunctionality of AtTRM5 and the importance of the post-transcriptional tRNA modifications m 1 G and m 1 I at tRNA position 37 in general plant growth and development.
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Metadata
- Authors
- Guo, Q., Ng, P., Shi, S., Fan, D., Li, J., Wang, H., Do, T., David, R., Mittal, P., Bock, R., Zhao, M., Zhou, W., & Searle, I. R.
- Affiliations
- Chinese Academy of Agricultural Sciences (CN)
- Shanghai Jiao Tong University (CN)
- Chinese Academy of Sciences (CN)
- ARC Centre of Excellence in Plant Energy Biology (AU)
- The University of Adelaide (AU)
- Max Planck Institute of Molecular Plant Physiology (DE)
- Corresponding author
- Zhou, W.
- Searle, I. R.
- Venue
- PLoS ONE
- Publisher
- openRxiv
- Published
- 2018-12-03
- Volume
- 14
- Issue
- 11
- Pages
- e0225064-e0225064
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC6874348
- OpenAlex
- W2989581388
- Cited by
- 25
- References
- 1
- Citations by year
- 2026: 2 · 2025: 7 · 2024: 2 · 2023: 2 · 2022: 5 · 2021: 6 · 2020: 1
- FWCI
- 0.99
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- PLoS ONE (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Adelaide Research & Scholarship (AR&S) (University of Adelaide) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Australian Cancer Research Foundation
- University of Adelaide
- National Natural Science Foundation of China (31570234)
- Chinese Academy of Agricultural Sciences
- Department of Industry, Innovation and Science, Australian Government (ACSRF48187)
- Australian Research Council (FT130100525)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Keywords
- Arabidopsis thaliana, plant growth, delayed flowering, leaf initiation, root length, photosynthetic proteins, nuclear localization
- MeSH terms
- Base Sequence, Cell Nucleus, Guanine, Inosine, Phenotype, Photosynthesis, tRNA Methyltransferases, Conserved Sequence, Genes, Plant, Arabidopsis, Gene Expression Regulation, Plant, Plant Leaves, Plant Roots, RNA, Plant, Arabidopsis Proteins, Flowers, Circadian Clocks
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