Evidence map›Paper›PMID 21858014›Full record

ArticlePloS one2011

Comprehensive structural and substrate specificity classification of the Saccharomyces cerevisiae methyltransferome.

Tomasz Wlodarski, Jan Kutner, Joanna Towpik, Lukasz Knizewski, Leszek Rychlewski, Andrzej Kudlicki, Maga Rowicka, Andrzej Dziembowski, Krzysztof Ginalski

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. 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
–field-weighted citation impact, top 100% 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, 0 citations in OpenAlex.

  1. Article
  2. Review
  3. Generation and characterization of two acid-resistant macrocinComputational and structural biotechnology journal · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Expanding the eukaryotic genetic code with a biosynthesized 21st amino acid.Protein science : a publication of the Protein Society · 2022
    Article
  9. Methyltransferases: Functions and Applications.Chembiochem : a European journal of chemical biology · 2022
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Network dynamics of the yeast methyltransferome.Microbial cell (Graz, Austria) · 2019
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
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

9 authors at 4 institutions in 2 countries.

Tomasz WlodarskiLaboratory of Bioinformatics and Systems Biology, Interdisciplinary Centre for Mathematical and Computational Modelling, University of Warsaw, Warsaw, Poland.
Jan Kutner
Joanna Towpik
Lukasz Knizewski
Leszek Rychlewski
Andrzej Kudlicki
Maga Rowicka
Andrzej Dziembowski
Krzysztof Ginalski
University of Warsaw · PLThe University of Texas Medical Branch at Galveston · USBioInfoBank Institute · PLInstitute of Biochemistry and Biophysics, Polish Academy of Sciences · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Methylation is one of the most common chemical modifications of biologically active molecules and it occurs in all life forms. Its functional role is very diverse and involves many essential cellular processes, such as signal transduction, transcriptional control, biosynthesis, and metabolism. Here, we provide further insight into the enzymatic methylation in S. cerevisiae by conducting a comprehensive structural and functional survey of all the methyltransferases encoded in its genome. Using distant homology detection and fold recognition, we found that the S. cerevisiae methyltransferome comprises 86 MTases (53 well-known and 33 putative with unknown substrate specificity). Structural classification of their catalytic domains shows that these enzymes may adopt nine different folds, the most common being the Rossmann-like. We also analyzed the domain architecture of these proteins and identified several new domain contexts. Interestingly, we found that the majority of MTase genes are periodically expressed during yeast metabolic cycle. This finding, together with calculated isoelectric point, fold assignment and cellular localization, was used to develop a novel approach for predicting substrate specificity. Using this approach, we predicted the general substrates for 24 of 33 putative MTases and confirmed these predictions experimentally in both cases tested. Finally, we show that, in S. cerevisiae, methylation is carried out by 34 RNA MTases, 32 protein MTases, eight small molecule MTases, three lipid MTases, and nine MTases with still unknown substrate specificity.

Indexed as

Catalytic DomainElectrophoresis, Polyacrylamide GelGenome, FungalMethylationMethyltransferasesMultigene FamilyMutationProteomeRNA, FungalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStructure-Activity RelationshipSubstrate SpecificityMethyltransferasesProteomeRNA, FungalSaccharomyces cerevisiae Proteins

Identifiers

PMID21858014
PMCPMC3153492
OpenAlexW23099290

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.