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Peer-reviewedCC BYNucleic Acids Research

Queuosine-modification dependent histidyl tRNA fragment promotes cell-type dependent proliferation

  • Wen Zhang1
  • Brandon J Chew2
  • Zaneta Matuszek1
  • Sihao Huang1
  • Luke R Frietze1
  • Hoang Anh V Tran1
  • Christopher D Katanski1
  • Marcus Foo3
  • Qing Dai1
  • Tao Pan1
  1. 1Department of Biochemistry and Molecular Biology, University of Chicago , Chicago, IL 60637 ,
  2. 2Department of Molecular Genetics and Cell Biology, University of Chicago , Chicago, IL 60637 ,
  3. 3Committee on Microbiology, University of Chicago , Chicago, IL 60637 ,
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Abstract

tRNA fragments (tRFs) are natural, small non-coding RNAs produced by endogenous ribonucleolytic cleavage of tRNAs. tRFs play a role in many biological pathways, including regulation of cell proliferation. Specific tRNA modifications affect tRF biogenesis. Queuosine (Q) modification occurs at the wobble anticodon nucleotide of 4 mammalian tRNAs and protects these tRNAs from fragmentation. Here, we investigated cell-type and tRNA Q-modification dependencies on mammalian cell proliferation. We found that Q-modified tRNA can either increase, decrease, or make no difference in proliferation. Proliferation decreased in MCF7, a breast cancer cell line, when tRNAs were Q-modified and dependent on the modification enzyme complex, QTRT1/2. MCF7 proliferation increases upon the transfection of Q-modification-dependent tRFHis or decreases upon knockdown of endogenous tRFHis. Consistent with Q-dependent proliferation reduction, polysome profiling showed decreased translation efficiency of ribosomal proteins. Finally, protein pull-down of MCF7 lysates using tRFHis identified Musashi RNA-binding protein 2 (Msi2) as a tRFHis-binding protein. Msi2 knockdown reduced the Q-modification-dependent or tRFHis dependent cell proliferation effect. Our results illustrate a highly cell-type-dependent proliferation effect of tRNA Q-modification, suggesting multi-faceted mechanisms in studying this ubiquitous tRNA modification.

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Cite

BibTeXRIS
BibTeX
@article{zhang2026queuosinemodification,
  title = {{Queuosine-modification dependent histidyl tRNA fragment promotes cell-type dependent proliferation}},
  author = {Wen Zhang and Brandon J Chew and Zaneta Matuszek and Sihao Huang and Luke R Frietze and Hoang Anh V Tran and Christopher D Katanski and Marcus Foo and Qing Dai and Tao Pan},
  journal = {Nucleic Acids Research},
  year = {2026},
  month = oct,
  doi = {10.1093/nar/gkag1101},
  url = {https://academic.oup.com/nar/article/doi/10.1093/nar/gkag1101/9005797},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - Queuosine-modification dependent histidyl tRNA fragment promotes cell-type dependent proliferation
AU  - Wen Zhang
AU  - Brandon J Chew
AU  - Zaneta Matuszek
AU  - Sihao Huang
AU  - Luke R Frietze
AU  - Hoang Anh V Tran
AU  - Christopher D Katanski
AU  - Marcus Foo
AU  - Qing Dai
AU  - Tao Pan
PY  - 2026
DA  - 2026/10/31
JO  - Nucleic Acids Research
DO  - 10.1093/nar/gkag1101
UR  - https://academic.oup.com/nar/article/doi/10.1093/nar/gkag1101/9005797
AB  - tRNA fragments (tRFs) are natural, small non-coding RNAs produced by endogenous ribonucleolytic cleavage of tRNAs. tRFs play a role in many biological pathways, including regulation of cell proliferation. Specific tRNA modifications affect tRF biogenesis. Queuosine (Q) modification occurs at the wobble anticodon nucleotide of 4 mammalian tRNAs and protects these tRNAs from fragmentation. Here, we investigated cell-type and tRNA Q-modification dependencies on mammalian cell proliferation. We found that Q-modified tRNA can either increase, decrease, or make no difference in proliferation. Proliferation decreased in MCF7, a breast cancer cell line, when tRNAs were Q-modified and dependent on the modification enzyme complex, QTRT1/2. MCF7 proliferation increases upon the transfection of Q-modification-dependent tRFHis or decreases upon knockdown of endogenous tRFHis. Consistent with Q-dependent proliferation reduction, polysome profiling showed decreased translation efficiency of ribosomal proteins. Finally, protein pull-down of MCF7 lysates using tRFHis identified Musashi RNA-binding protein 2 (Msi2) as a tRFHis-binding protein. Msi2 knockdown reduced the Q-modification-dependent or tRFHis dependent cell proliferation effect. Our results illustrate a highly cell-type-dependent proliferation effect of tRNA Q-modification, suggesting multi-faceted mechanisms in studying this ubiquitous tRNA modification.
SN  - 0305-1048
SN  - 1362-4962
ER  -