Evidence map›Paper›PMID 25925947›Full record

ArticleThe Journal of biological chemistry2015

OlsG (Sinac_1600) Is an Ornithine Lipid N-Methyltransferase from the Planctomycete Singulisphaera acidiphila.

Wendy Itzel Escobedo-Hinojosa, Miguel Ángel Vences-Guzmán, Florence Schubotz, Mario Sandoval-Calderón, Roger E Summons, Isabel María López-Lara, Otto Geiger, Christian Sohlenkamp

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

10 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Genome Analysis of Fimbriiglobus ruber SP5Applied and environmental microbiology · 2018
    Article
  8. Lipid Profile ofFrontiers in microbiology · 2018
    Article
  9. Article
  10. 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

8 authors at 2 institutions in 2 countries.

Wendy Itzel Escobedo-HinojosaFrom the Centro de Ciencias Genómicas, Universidad Nacional Autónoma de México, Cuernavaca, Morelos CP62210, Mexico and.
Miguel Ángel Vences-GuzmánFrom the Centro de Ciencias Genómicas, Universidad Nacional Autónoma de México, Cuernavaca, Morelos CP62210, Mexico and.
Florence Schubotzthe Department of Earth, Atmospheric and Planetary Sciences, Massachusetts Institute of Technology, Cambridge, Massachusetts 02144.
Mario Sandoval-CalderónFrom the Centro de Ciencias Genómicas, Universidad Nacional Autónoma de México, Cuernavaca, Morelos CP62210, Mexico and.
Roger E Summonsthe Department of Earth, Atmospheric and Planetary Sciences, Massachusetts Institute of Technology, Cambridge, Massachusetts 02144.
Isabel María López-LaraFrom the Centro de Ciencias Genómicas, Universidad Nacional Autónoma de México, Cuernavaca, Morelos CP62210, Mexico and.
Otto GeigerFrom the Centro de Ciencias Genómicas, Universidad Nacional Autónoma de México, Cuernavaca, Morelos CP62210, Mexico and.
Christian SohlenkampFrom the Centro de Ciencias Genómicas, Universidad Nacional Autónoma de México, Cuernavaca, Morelos CP62210, Mexico and chsohlen@ccg.unam.mx.ORCID http://orcid.org/0000-0002-9962-2859
Universidad Nacional Autónoma de México · MXMassachusetts Institute of Technology · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ornithine lipids (OLs) are phosphorus-free membrane lipids widespread in bacteria but absent from archaea and eukaryotes. In addition to the unmodified OLs, a variety of OL derivatives hydroxylated in different structural positions has been reported. Recently, methylated derivatives of OLs were described in several planctomycetes isolated from a peat bog in Northern Russia, although the gene/enzyme responsible for the N-methylation of OL remained obscure. Here we identify and characterize the OL N-methyltransferase OlsG (Sinac_1600) from the planctomycete Singulisphaera acidiphila. When OlsG is co-expressed with the OL synthase OlsF in Escherichia coli, methylated OL derivatives are formed. An in vitro characterization shows that OlsG is responsible for the 3-fold methylation of the terminal δ-nitrogen of OL. Methylation is dependent on the presence of the detergent Triton X-100 and the methyldonor S-adenosylmethionine.

Indexed as

Base SequenceChromatography, High Pressure LiquidCloning, MolecularDNA PrimersEscherichia coliLipidsMass SpectrometryMembrane LipidsMethyltransferasesOrnithinePhylogenyPlanctomycetalesDNA PrimersLipidsMembrane LipidsMethyltransferasesOrnithineornithine containing aminolipidlipid methylationmembrane lipidmembrane remodelingphosphatidylcholine

Identifiers

PMID25925947
PMCPMC4463453
OpenAlexW1984699583

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.