Evidence map›Paper›PMID 30902983›Full record

ArticleNature communications2019

A threonyl-tRNA synthetase-mediated translation initiation machinery.

Seung Jae Jeong, Shinhye Park, Loi T Nguyen, Jungwon Hwang, Eun-Young Lee, Hoi-Khoanh Giong, Jeong-Soo Lee, Ina Yoon, Ji-Hyun Lee, Jong Hyun Kim and 9 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

44 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
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  8. Circadian Control of Protein Synthesis.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
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  9. The role of m5C, m1A and m7G modifications in tumors of urinary system.Frontiers in cell and developmental biology · 2025
    Review
  10. Review
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  14. Review
  15. Article
  16. Article
  17. RNA modifications in cancer.British journal of cancer · 2023
    Review
  18. Article
  19. Article
  20. Article
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

19 authors at 6 institutions in 4 countries.

Seung Jae JeongMedicinal Bioconvergence Research Center, Seoul National University, Suwon, 16229, Korea.
Shinhye ParkInfection and Immunity Research Laboratory, Metabolic Regulation Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, 34141, Korea.
Loi T NguyenInfection and Immunity Research Laboratory, Metabolic Regulation Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, 34141, Korea.
Jungwon HwangInfection and Immunity Research Laboratory, Metabolic Regulation Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, 34141, Korea.ORCID http://orcid.org/0000-0002-4628-6177
Eun-Young LeeInfection and Immunity Research Laboratory, Metabolic Regulation Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, 34141, Korea.
Hoi-Khoanh GiongDisease Target Structure Research Center, KRIBB, Daejeon, 34141, Korea.
Jeong-Soo LeeDisease Target Structure Research Center, KRIBB, Daejeon, 34141, Korea.
Ina YoonMedicinal Bioconvergence Research Center, Seoul National University, Suwon, 16229, Korea.
Ji-Hyun LeeMedicinal Bioconvergence Research Center, Seoul National University, Suwon, 16229, Korea.
Jong Hyun KimMedicinal Bioconvergence Research Center, Seoul National University, Suwon, 16229, Korea.
Hoi Kyoung KimMedicinal Bioconvergence Research Center, Seoul National University, Suwon, 16229, Korea.
Doyeun KimMedicinal Bioconvergence Research Center, Seoul National University, Suwon, 16229, Korea.
Won Suk YangMedicinal Bioconvergence Research Center, Seoul National University, Suwon, 16229, Korea.
Seon-Young KimKRIBB School of Bioscience, Korea University of Science and Technology, Daejeon, 34141, Korea.ORCID http://orcid.org/0000-0002-1030-7730
Chan Yong LeeDepartment of Biochemistry, Chungnam National University, Daejeon, 34134, Korea.
Kweon YuDisease Target Structure Research Center, KRIBB, Daejeon, 34141, Korea.ORCID http://orcid.org/0000-0002-4942-2576
Nahum SonenbergDepartment of Biochemistry, McGill University, Montreal, Quebec, H3A 1A3, Canada.
Myung Hee KimInfection and Immunity Research Laboratory, Metabolic Regulation Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, 34141, Korea. mhk8n@kribb.re.kr.
Sunghoon KimMedicinal Bioconvergence Research Center, Seoul National University, Suwon, 16229, Korea. sungkim@snu.ac.kr.ORCID http://orcid.org/0000-0002-1570-3230
Seoul National University · KRKorea Research Institute of Bioscience and Biotechnology · KRChungnam National University · KRConvergence Research Center for Diagnosis Treatment and Care System of Dementia · KRBiocon (Switzerland) · CHOccupational Cancer Research Centre · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A fundamental question in biology is how vertebrates evolved and differ from invertebrates, and little is known about differences in the regulation of translation in the two systems. Herein, we identify a threonyl-tRNA synthetase (TRS)-mediated translation initiation machinery that specifically interacts with eIF4E homologous protein, and forms machinery that is structurally analogous to the eIF4F-mediated translation initiation machinery via the recruitment of other translation initiation components. Biochemical and RNA immunoprecipitation analyses coupled to sequencing suggest that this machinery emerged as a gain-of-function event in the vertebrate lineage, and it positively regulates the translation of mRNAs required for vertebrate development. Collectively, our findings demonstrate that TRS evolved to regulate vertebrate translation initiation via its dual role as a scaffold for the assembly of initiation components and as a selector of target mRNAs. This work highlights the functional significance of aminoacyl-tRNA synthetases in the emergence and control of higher order organisms.

Indexed as

Peptide Chain Initiation, TranslationalAmino Acid SequenceAnimalsBlood VesselsEukaryotic Initiation Factor-4EEukaryotic Initiation Factor-4FEukaryotic Initiation Factor-4GHEK293 CellsHumansHuman Umbilical Vein Endothelial CellsMice, Inbred C57BLProtein BindingRNA Cap-Binding ProteinsRNA, MessengerSpecies SpecificityThreonine-tRNA LigaseEIF4E2 protein, humanEukaryotic Initiation Factor-4EEukaryotic Initiation Factor-4FEukaryotic Initiation Factor-4GRNA Cap-Binding ProteinsRNA, MessengerThreonine-tRNA Ligase

Identifiers

PMID30902983
PMCPMC6430810
OpenAlexW2923362859

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.