Evidence map›Paper›PMID 32678822›Full record

ArticlePloS one2020

Evolutionary conservation and post-translational control of S-adenosyl-L-homocysteine hydrolase in land plants.

Sara Alegre, Jesús Pascual, Andrea Trotta, Martina Angeleri, Moona Rahikainen, Mikael Brosche, Barbara Moffatt, Saijaliisa Kangasjärvi

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

11 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Posttranslational Regulation of Mammalian Sulfur Amino Acid Metabolism.International journal of molecular sciences · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Metabolism and Regulatory Functions ofFrontiers in plant science · 2021
    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

8 authors at 3 institutions in 3 countries.

Sara AlegreDepartment of Biochemistry, Molecular Plant Biology, University of Turku, Turku, Finland.ORCID 0000-0001-7893-2711
Jesús PascualDepartment of Biochemistry, Molecular Plant Biology, University of Turku, Turku, Finland.
Andrea TrottaDepartment of Biochemistry, Molecular Plant Biology, University of Turku, Turku, Finland.ORCID 0000-0002-3660-5090
Martina AngeleriDepartment of Biochemistry, Molecular Plant Biology, University of Turku, Turku, Finland.
Moona RahikainenDepartment of Biochemistry, Molecular Plant Biology, University of Turku, Turku, Finland.ORCID 0000-0001-5365-8963
Mikael BroscheOrganismal and Evolutionary Biology Research Program, Faculty of Biological and Environmental Sciences, Viikki Plant Science Centre, University of Helsinki, Helsinki, Finland.
Barbara MoffattDepartment of Biology, University of Waterloo, Waterloo, Ontario, Canada.
Saijaliisa KangasjärviDepartment of Biochemistry, Molecular Plant Biology, University of Turku, Turku, Finland.ORCID 0000-0002-7605-8546
University of Turku · FIUniversity of Helsinki · FIUniversity of Waterloo · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Trans-methylation reactions are intrinsic to cellular metabolism in all living organisms. In land plants, a range of substrate-specific methyltransferases catalyze the methylation of DNA, RNA, proteins, cell wall components and numerous species-specific metabolites, thereby providing means for growth and acclimation in various terrestrial habitats. Trans-methylation reactions consume vast amounts of S-adenosyl-L-methionine (SAM) as a methyl donor in several cellular compartments. The inhibitory reaction by-product, S-adenosyl-L-homocysteine (SAH), is continuously removed by SAH hydrolase (SAHH), which essentially maintains trans-methylation reactions in all living cells. Here we report on the evolutionary conservation and post-translational control of SAHH in land plants. We provide evidence suggesting that SAHH forms oligomeric protein complexes in phylogenetically divergent land plants and that the predominant protein complex is composed by a tetramer of the enzyme. Analysis of light-stress-induced adjustments of SAHH in Arabidopsis thaliana and Physcomitrella patens further suggests that regulatory actions may take place on the levels of protein complex formation and phosphorylation of this metabolically central enzyme. Collectively, these data suggest that plant adaptation to terrestrial environments involved evolution of regulatory mechanisms that adjust the trans-methylation machinery in response to environmental cues.

Indexed as

Evolution, MolecularAdenosylhomocysteinaseAmino Acid SequenceArabidopsisArabidopsis ProteinsElectrophoresis, Gel, Two-DimensionalIsoelectric FocusingLightPhylogenyPlant LeavesProtein Processing, Post-TranslationalRNA, MessengerSequence AlignmentStress, PhysiologicalAdenosylhomocysteinaseArabidopsis ProteinsRNA, Messenger

Identifiers

PMID32678822
PMCPMC7367456
OpenAlexW3043608298

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.