Evidence map›Paper›PMID 11115895›Full record

ArticlePlant physiology2000

The isolation and characterization in yeast of a gene for Arabidopsis S-adenosylmethionine:phospho-ethanolamine N-methyltransferase.

C P Bolognese, P McGraw

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

44 citing papers in PubMed, 86 citations in OpenAlex.

  1. A Comprehensive Functional Analysis ofPlants (Basel, Switzerland) · 2025
    Article
  2. Article
  3. Article
  4. uORFs: ImportantInternational journal of molecular sciences · 2020
    Review
  5. Article
  6. Article
  7. Article
  8. Loss of PhosphoethanolaminePlant physiology · 2019
    Article
  9. Article
  10. NMT1 and NMT3Plant physiology · 2018
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Conformational changes in the di-domain structure ofThe Journal of biological chemistry · 2017
    Article
  16. Review
  17. Article
  18. Article
  19. Article
  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

2 authors at 1 institution in 1 country.

C P BologneseDepartment of Biological Sciences, University of Maryland, Baltimore, Maryland 21250, USA.
P McGraw
University of Maryland, Baltimore · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Saccharomyces cerevisiae opi3 mutant strains do not have the phospholipid N-methyltransferase that catalyzes the two terminal methylations in the phosphatidylcholine (PC) biosynthetic pathway. This results in a build up of the intermediate phosphatidylmonomethylethanolamine, causing a temperature-sensitive growth phenotype. An Arabidopsis cDNA library was used to isolate three overlapping plasmids that complemented the temperature-sensitive phenotype. Phospholipid analysis showed that the presence of the cloned cDNA caused a 65-fold reduction in the level of phosphatidylmonomethylethanolamine and a significant, though not equivalent, increase in the production of PC. Sequence analysis established that the cDNA was not homologous to OPI3 or to CHO2, the only other yeast phospholipid N-methyltransferase, but was similar to several other classes of methyltransferases. S-adenosyl-Met:phospho-base N-methyltransferase assays revealed that the cDNA catalyzed the three sequential methylations of phospho-ethanolamine to form phospho-choline. Phospho-choline is converted to PC by the CDP-choline pathway, explaining the phenotype conferred upon the yeast mutant strain by the cDNA. In accordance with this the gene has been named AtNMT1. The identification of this enzyme and the failure to isolate a plant phospholipid N-methyltransferase suggests that there are fundamental differences between the pathways utilized by yeast and by some plants for synthesis of PC.

Indexed as

Arabidopsis ProteinsAmino Acid SequenceArabidopsisBase SequenceDNA, ComplementaryGenetic Complementation TestMethyltransferasesMolecular Sequence DataMutationPhenotypePhospholipidsSaccharomyces cerevisiaeS-AdenosylmethionineSequence AlignmentSequence Analysis, DNASequence Homology, Amino AcidArabidopsis Proteinsat3g18000 protein, ArabidopsisDNA, ComplementaryMethyltransferasesPhospholipidsS-Adenosylmethionine

Identifiers

PMID11115895
PMCPMC59876
OpenAlexW2043878188

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.