ArticleMolecular and cellular biology2013
Human cells have a limited set of tRNA anticodon loop substrates of the tRNA isopentenyltransferase TRIT1 tumor suppressor.
Article in Molecular and cellular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 47 citations in OpenAlex.
- Advanced computational approaches to understand protein aggregation.Biophysics reviews · 2024Review
- Fit for Purpose Approach To Evaluate Detection of Amino Acid Substitutions in Shotgun Proteomics.Journal of proteome research · 2024Article
- A tRNA modifying enzyme as a tunable regulatory nexus for bacterial stress responses and virulence.Nucleic acids research · 2022Article
- ExtracellularRNA (New York, N.Y.) · 2022Article
- Molecular basis for human mitochondrial tRNA m3C modification by alternatively spliced METTL8.Nucleic acids research · 2022Article
- A versatile tRNA modification-sensitive northern blot method with enhanced performance.RNA (New York, N.Y.) · 2022Article
- Balancing of mitochondrial translation through METTL8-mediated mMolecular cell · 2021Article
- Modifications of the human tRNA anticodon loop and their associations with genetic diseases.Cellular and molecular life sciences : CMLS · 2021Review
- The Importance of the Epi-Transcriptome in Translation Fidelity.Non-coding RNA · 2021Review
- Failure to Guard: Mitochondrial Protein Quality Control in Cancer.International journal of molecular sciences · 2021Review
- Targeting the Mevalonate Pathway in Cancer.Trends in cancer · 2021Review
- Article
- Disruption of the RNA modifications that target the ribosome translation machinery in human cancer.Molecular cancer · 2020Review
- Targeting mitochondrial and cytosolic substrates of TRIT1 isopentenyltransferase: Specificity determinants and tRNA-i6A37 profiles.PLoS genetics · 2020Article
- The Origins and Roles of Methylthiolated Cytokinins: Evidence From Among Life Kingdoms.Frontiers in cell and developmental biology · 2020Review
- Phytohormone metabolism in human cells: Cytokinins are taken up and interconverted in HeLa cell culture.FASEB bioAdvances · 2019Article
- Gene ssfg_01967 (miaB) for tRNA modification influences morphogenesis and moenomycin biosynthesis in Streptomyces ghanaensis ATCC14672.Microbiology (Reading, England) · 2019Article
- An In Vitro Assay to Detect tRNA-Isopentenyl Transferase Activity.Journal of visualized experiments : JoVE · 2018Article
- The tRNA biology · 2018Article
- Protein folding and tRNA biology.Biophysical reviews · 2017Review
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3 authors at 1 institution in 1 country.
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Abstract
Human TRIT1 is a tRNA isopentenyltransferase (IPTase) homologue of Escherichia coli MiaA, Saccharomyces cerevisiae Mod5, Schizosaccharomyces pombe Tit1, and Caenorhabditis elegans GRO-1 that adds isopentenyl groups to adenosine 37 (i6A37) of substrate tRNAs. Prior studies indicate that i6A37 increases translation fidelity and efficiency in codon-specific ways. TRIT1 is a tumor suppressor whose mutant alleles are associated with cancer progression. We report the systematic identification of i6A37-containing tRNAs in a higher eukaryote, performed using small interfering RNA knockdown and other methods to examine TRIT1 activity in HeLa cells. Although several potential substrates contained the IPTase recognition sequence A36A37A38 in the anticodon loop, only tRNA(Ser)AGA, tRNA(Ser)CGA, tRNA(Ser)UGA, and selenocysteine tRNA with UCA (tRNA([Ser]Sec)UCA) contained i6A37. This subset is a significantly more restricted than that for two distant yeasts (S. cerevisiae and S. pombe), the only other organisms comprehensively examined. Unlike the fully i6A37-modified tRNAs for Ser, tRNA([Ser]Sec)UCA is partially (∼40%) modified. Exogenous selenium and other treatments that decreased the i6A37 content of tRNA([Ser]Sec)UCA led to increased levels of the tRNA([Ser]Sec)UCA. Of the human mitochondrion (mt)-encoded tRNAs with A36A37A38, only mt tRNAs tRNA(Ser)UGA and tRNA(Trp)UCA contained detectable i6A37. Moreover, while tRNA(Ser) levels were unaffected by TRIT1 knockdown, the tRNA([Ser]Sec)UCA level was increased and the mt tRNA(Ser)UGA level was decreased, suggesting that TRIT1 may control the levels of some tRNAs as well as their specific activity.
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