Evidence map›Paper›PMID 17242307›Full record

ArticleRNA (New York, N.Y.)2007

The 2'-O-methyltransferase responsible for modification of yeast tRNA at position 4.

Martha L Wilkinson, Sharon M Crary, Jane E Jackman, Elizabeth J Grayhack, Eric M Phizicky

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

34 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Review
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  5. Article
  6. Article
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  8. Article
  9. Review
  10. Review
  11. Epitranscriptome: Review of Top 25 Most-Studied RNA Modifications.International journal of molecular sciences · 2022
    Review
  12. Developmental roles and molecular mechanisms of Asterix/GTSF1.Wiley interdisciplinary reviews. RNA · 2022
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. A Census and Categorization Method of Epitranscriptomic Marks.International journal of molecular sciences · 2020
    Review
  18. Article
  19. Article
  20. Review
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

5 authors at 2 institutions in 1 country.

Martha L WilkinsonDepartment of Biochemistry, University of Rochester School of Medicine, NY 14642, USA.
Sharon M Crary
Jane E Jackman
Elizabeth J Grayhack
Eric M Phizicky
University of Rochester · USDePauw University · US

Funding

TRNA SPLICINGR01GM052347 · NIGMS · UNIVERSITY OF ROCHESTER · PI Eric M. Phizicky · 1995 to 2026
$9.6M
NIGMS NIH HHS GM52347NIGMS NIH HHS R01 GM052347
6 · The paper itself

Abstract

The methylation of the ribose 2'-OH of RNA occurs widely in nature and in all stable RNAs and occurs at five positions in yeast tRNA. 2'-O-methylation of tRNA at position 4 is interesting because it occurs in the acceptor stem (which is normally undermodified), it is the only 2'-O-methylation that occurs in the middle of a duplex region in tRNA, the modification is conserved in eukaryotes, and the features of the tRNA necessary for substrate recognition are poorly defined. We show here that Saccharomyces cerevisiae ORF YOL125w (TRM13) is necessary and sufficient for 2'-O-methylation at position 4 of yeast tRNA. Biochemical analysis of the S. cerevisiae proteome shows that Trm13 copurifies with 2'-O-methylation activity, using tRNAGlyGCC as a substrate, and extracts made from a trm13-Delta strain have undetectable levels of this activity. Trm13 is necessary for activity in vivo because tRNAs isolated from a trm13-Delta strain lack the corresponding 2'-O-methylated residue for each of the three known tRNAs with this modification. Trm13 is sufficient for 2'-O-methylation at position 4 in vitro since yeast Trm13 protein purified after expression in Escherichia coli has the same activity as that produced in yeast. Trm13 protein binds substrates tRNAHis and tRNAGlyGCC with KD values of 85+/-8 and 100+/-14 nM, respectively, and has a KM for tRNAHis of 10 nM, but binds nonsubstrate tRNAs very poorly (KD>1 microM). Trm13 is conserved in eukaryotes, but there is no sequence similarity between Trm13 and other known methyltransferases.

Indexed as

Amino Acid SequenceMethylationMolecular Sequence DataNucleic Acid ConformationRNA, FungalRNA, Transfer, Amino AcylSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmenttRNA MethyltransferasesRNA, FungalRNA, Transfer, Amino AcylSaccharomyces cerevisiae ProteinsTRM13 protein, S cerevisiaetRNA Methyltransferases

Identifiers

PMID17242307
PMCPMC1800514
OpenAlexW2154360219

What OpenQuestion holds

Textmetadata
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.