ArticleMolecular and cellular biology2007
Thio modification of yeast cytosolic tRNA is an iron-sulfur protein-dependent pathway.
Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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.
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.
Who cites it
33 citing papers in PubMed, 66 citations in OpenAlex.
- Yeast Mitochondria Import Aqueous FeJournal of the American Chemical Society · 2023Article
- Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2.Molecules (Basel, Switzerland) · 2022Review
- Sulfur modification in natural RNA and therapeutic oligonucleotides.RSC chemical biology · 2021Review
- Urm1: A Non-Canonical UBL.Biomolecules · 2021Review
- tRNA wobble-uridine modifications as amino acid sensors and regulators of cellular metabolic state.Current genetics · 2020Review
- Roles of Elongator Dependent tRNA Modification Pathways in Neurodegeneration and Cancer.Genes · 2018Review
- Mitochondria Export Sulfur Species Required for Cytosolic tRNA Thiolation.Cell chemical biology · 2018Article
- Recent Advances in Our Understanding of the Biosynthesis of Sulfur Modifications in tRNAs.Frontiers in microbiology · 2018Article
- Wobble uridine modifications-a reason to live, a reason to die?!RNA biology · 2017Review
- Biochemical and structural characterization of oxygen-sensitive 2-thiouridine synthesis catalyzed by an iron-sulfur protein TtuA.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Biosynthesis of Sulfur-Containing tRNA Modifications: A Comparison of Bacterial, Archaeal, and Eukaryotic Pathways.Biomolecules · 2017Review
- Sulfur Modifications of the Wobble UBiomolecules · 2017Review
- A [3Fe-4S] cluster is required for tRNA thiolation in archaea and eukaryotes.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Glutaredoxin GRXS17 Associates with the Cytosolic Iron-Sulfur Cluster Assembly Pathway.Plant physiology · 2016Article
- Defining the orphan functions of lysine acetyltransferases.ACS chemical biology · 2015Review
- Mammalian iron-sulphur proteins: novel insights into biogenesis and function.Nature reviews. Molecular cell biology · 2015Review
- Characterization and interaction studies of two isoforms of the dual localized 3-mercaptopyruvate sulfurtransferase TUM1 from humans.The Journal of biological chemistry · 2014Article
- Mitochondrial and nucleolar localization of cysteine desulfurase Nfs and the scaffold protein Isu in Trypanosoma brucei.Eukaryotic cell · 2014Article
- Biosynthesis and functions of sulfur modifications in tRNA.Frontiers in genetics · 2014Review
- Elongator, a conserved complex required for wobble uridine modifications in eukaryotes.RNA biology · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Defects in the yeast cysteine desulfurase Nfs1 cause a severe impairment in the 2-thio modification of uridine of mitochondrial tRNAs (mt-tRNAs) and cytosolic tRNAs (cy-tRNAs). Nfs1 can also provide the sulfur atoms of the iron-sulfur (Fe/S) clusters generated by the mitochondrial and cytosolic Fe/S cluster assembly machineries, termed ISC and CIA, respectively. Therefore, a key question remains as to whether the biosynthesis of Fe/S clusters is a prerequisite for the 2-thio modification of the tRNAs in both of the subcellular compartments of yeast cells. To elucidate this question, we asked whether mitochondrial ISC and/or cytosolic CIA components besides Nfs1 were involved in the 2-thio modification of these tRNAs. We demonstrate here that the three CIA components, Cfd1, Nbp35, and Cia1, are required for the 2-thio modification of cy-tRNAs but not of mt-tRNAs. Interestingly, the mitochondrial scaffold proteins Isu1 and Isu2 are required for the 2-thio modification of the cy-tRNAs but not of the mt-tRNAs, while mitochondrial Nfs1 is required for both 2-thio modifications. These results clearly indicate that the 2-thio modification of cy-tRNAs is Fe/S protein dependent and thus requires both CIA and ISC machineries but that of mt-tRNAs is Fe/S cluster independent and does not require key mitochondrial ISC components except for Nfs1.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.