ArticleNucleic acids research2007
Conserved amino acids in each subunit of the heteroligomeric tRNA m1A58 Mtase from Saccharomyces cerevisiae contribute to tRNA binding.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.
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Who cites it
25 citing papers in PubMed, 1 synthesis or guideline pooled it, 35 citations in OpenAlex.
- Meta-analysis of small RNA-sequencing errors reveals ubiquitous post-transcriptional RNA modifications.Nucleic acids research · 2009Pooled it
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- The thiolation of uridine 34 in tRNA, which controls protein translation, depends on a [4Fe-4S] cluster in the archaeum Methanococcus maripaludis.Scientific reports · 2023Article
- Initiator tRNA lacking 1-methyladenosine is targeted by the rapid tRNA decay pathway in evolutionarily distant yeast species.PLoS genetics · 2022Article
- TRM61 is essential for Arabidopsis embryo and endosperm development.Plant reproduction · 2022Article
- THUMPD3-TRMT112 is a m2G methyltransferase working on a broad range of tRNA substrates.Nucleic acids research · 2021Article
- The NPlant physiology · 2020Article
- Multi-Substrate Specificity and the Evolutionary Basis for Interdependence in tRNA Editing and Methylation Enzymes.Frontiers in genetics · 2019Review
- Binding synergy as an essential step for tRNA editing and modification enzyme codependence inRNA (New York, N.Y.) · 2018Article
- Identification of tRNA nucleoside modification genes critical for stress response and development in rice and Arabidopsis.BMC plant biology · 2017Article
- The emerging biology of RNA post-transcriptional modifications.RNA biology · 2017Review
- Crystal structure of the two-subunit tRNA m(1)A58 methyltransferase TRM6-TRM61 from Saccharomyces cerevisiae.Scientific reports · 2016Article
- Crystal Structure of the Human tRNA m(1)A58 Methyltransferase-tRNA(3)(Lys) Complex: Refolding of Substrate tRNA Allows Access to the Methylation Target.Journal of molecular biology · 2015Article
- Diversity in mechanism and function of tRNA methyltransferases.RNA biology · 2015Review
- Two-subunit enzymes involved in eukaryotic post-transcriptional tRNA modification.RNA biology · 2014Review
- Methylated nucleosides in tRNA and tRNA methyltransferases.Frontiers in genetics · 2014Review
- Trmt61B is a methyltransferase responsible for 1-methyladenosine at position 58 of human mitochondrial tRNAs.RNA (New York, N.Y.) · 2012Article
- Yeast Trm7 interacts with distinct proteins for critical modifications of the tRNAPhe anticodon loop.RNA (New York, N.Y.) · 2012Article
- Structural comparison of tRNA m(1)A58 methyltransferases revealed different molecular strategies to maintain their oligomeric architecture under extreme conditions.BMC structural biology · 2011Article
- Crystallization and preliminary X-ray diffraction crystallographic study of tRNA m(1)A58 methyltransferase from Saccharomyces cerevisiae.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
In Saccharomyces cerevisiae, a two-subunit methyltransferase (Mtase) encoded by the essential genes TRM6 and TRM61 is responsible for the formation of 1-methyladenosine, a modified nucleoside found at position 58 in tRNA that is critical for the stability of tRNA(Met)i The crystal structure of the homotetrameric m1A58 tRNA Mtase from Mycobacterium tuberculosis, TrmI, has been solved and was used as a template to build a model of the yeast m1A58 tRNA Mtase heterotetramer. We altered amino acids in TRM6 and TRM61 that were predicted to be important for the stability of the heteroligomer based on this model. Yeast strains expressing trm6 and trm61 mutants exhibited growth phenotypes indicative of reduced m1A formation. In addition, recombinant mutant enzymes had reduced in vitro Mtase activity. We demonstrate that the mutations introduced do not prevent heteroligomer formation and do not disrupt binding of the cofactor S-adenosyl-L-methionine. Instead, amino acid substitutions in either Trm6p or Trm61p destroy the ability of the yeast m1A58 tRNA Mtase to bind tRNA(Met)i, indicating that each subunit contributes to tRNA binding and suggesting a structural alteration of the substrate-binding pocket occurs when these mutations are present.
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