Evidence map›Paper›PMID 34669960›Full record

ArticleNucleic acids research2021

THUMPD3-TRMT112 is a m2G methyltransferase working on a broad range of tRNA substrates.

Wen-Qing Yang, Qing-Ping Xiong, Jian-Yang Ge, Hao Li, Wen-Yu Zhu, Yan Nie, Xiuying Lin, Daizhu Lv, Jing Li, Huan Lin and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.4field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

47 citing papers in PubMed, 60 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 4 institutions in 1 country.

Wen-Qing YangSchool of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.
Qing-Ping XiongCAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences; University of Chinese Academy of Sciences, Shanghai 200031, China.
Jian-Yang GeSchool of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.
Hao LiSchool of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.
Wen-Yu ZhuSchool of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.
Yan NieShanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, Shanghai 201210, China.ORCID 0000-0003-2521-8519
Xiuying LinState Key Laboratory of Marine Resource Utilization in South China Sea, Hainan University, Haikou, China.
Daizhu LvAnalysis and Testing Center, Chinese Academy of Tropical Agricultural Sciences, Haikou 571101, China.
Jing LiSchool of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.
Huan LinState Key Laboratory of Marine Resource Utilization in South China Sea, Hainan University, Haikou, China.
Ru-Juan LiuSchool of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.ORCID 0000-0001-7459-3126
ShanghaiTech University · CNHainan University · CNCenter for Excellence in Molecular Cell Science · CNChinese Academy of Tropical Agricultural Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post-transcriptional modifications affect tRNA biology and are closely associated with human diseases. However, progress on the functional analysis of tRNA modifications in metazoans has been slow because of the difficulty in identifying modifying enzymes. For example, the biogenesis and function of the prevalent N2-methylguanosine (m2G) at the sixth position of tRNAs in eukaryotes has long remained enigmatic. Herein, using a reverse genetics approach coupled with RNA-mass spectrometry, we identified that THUMP domain-containing protein 3 (THUMPD3) is responsible for tRNA: m2G6 formation in human cells. However, THUMPD3 alone could not modify tRNAs. Instead, multifunctional methyltransferase subunit TRM112-like protein (TRMT112) interacts with THUMPD3 to activate its methyltransferase activity. In the in vitro enzymatic assay system, THUMPD3-TRMT112 could methylate all the 26 tested G6-containing human cytoplasmic tRNAs by recognizing the characteristic 3'-CCA of mature tRNAs. We also showed that m2G7 of tRNATrp was introduced by THUMPD3-TRMT112. Furthermore, THUMPD3 is widely expressed in mouse tissues, with an extremely high level in the testis. THUMPD3-knockout cells exhibited impaired global protein synthesis and reduced growth. Our data highlight the significance of the tRNA: m2G6/7 modification and pave a way for further studies of the role of m2G in sperm tRNA derived fragments.

Indexed as

HEK293 CellsHeLa CellsHumansMethylationMethyltransferasesRNA-Binding ProteinsRNA Processing, Post-TranscriptionalRNA, TransferSubstrate SpecificitytRNA MethyltransferasesMethyltransferasesRNA-Binding ProteinsRNA, TransferTHUMPD3 protein, humanTRMT112 protein, humantRNA Methyltransferases

Identifiers

PMID34669960
PMCPMC8599901
OpenAlexW3207617045

What OpenQuestion holds

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Registered trials

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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 OpenQuestion graph.