Evidence map›Paper›PMID 23852866›Full record

ArticleJournal of bacteriology2013

Identification of a mycoloyl transferase selectively involved in O-acylation of polypeptides in Corynebacteriales.

Emilie Huc, Célia de Sousa-D'Auria, Inès Li de la Sierra-Gallay, Christophe Salmeron, Herman van Tilbeurgh, Nicolas Bayan, Christine Houssin, Mamadou Daffé, Maryelle Tropis

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.6field-weighted citation impact, top 32% 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

13 citing papers in PubMed, 37 citations in OpenAlex.

  1. The mycomembrane proteins PorH and ProtX are inserted at polar growth zones and linked to the cell wall.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  7. Review
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  10. Tailoring Trehalose for Biomedical and Biotechnological Applications.Pure and applied chemistry. Chimie pure et appliquee · 2017
    Article
  11. Article
  12. Identification of specific posttranslationalProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  13. 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 2 institutions in 1 country.

Emilie HucTeam Enveloppes Mycobactériennes, Structure Biosynthèse et Rôles, Centre National de la Recherche Scientifique (CNRS), Institut de Pharmacologie et Biologie Structurale (IPBS), Département Mécanismes Moléculaires des Infections Mycobactériennes, UMR 5089, Toulouse, France.
Célia de Sousa-D'Auria
Inès Li de la Sierra-Gallay
Christophe Salmeron
Herman van Tilbeurgh
Nicolas Bayan
Christine Houssin
Mamadou Daffé
Maryelle Tropis
Université Paris-Sud · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have previously described the posttranslational modification of pore-forming small proteins of Corynebacterium by mycolic acid, a very-long-chain α-alkyl and β-hydroxy fatty acid. Using a combination of chemical analyses and mass spectrometry, we identified the mycoloyl transferase (Myt) that catalyzes the transfer of the fatty acid residue to yield O-acylated polypeptides. Inactivation of corynomycoloyl transferase C (cg0413 [Corynebacterium glutamicum mytC {CgmytC}]), one of the six Cgmyt genes of C. glutamicum, specifically abolished the O-modification of the pore-forming proteins PorA and PorH, which is critical for their biological activity. Expectedly, complementation of the cg0413 mutant with either the wild-type gene or its orthologues from Corynebacterium diphtheriae and Rhodococcus, but not Nocardia, fully restored the O-acylation of the porins. Consistently, the three-dimensional structure of CgMytC showed the presence of a unique loop that is absent from enzymes that transfer mycoloyl residues onto both trehalose and the cell wall arabinogalactan. These data suggest the implication of this structure in the enzyme specificity for protein instead of carbohydrate.

Indexed as

AcylationAcyltransferasesAmino Acid SequenceBacterial ProteinsCorynebacterium glutamicumModels, MolecularMolecular Sequence DataMycolic AcidsPeptidesPorinsSubstrate SpecificityAcyltransferasesBacterial ProteinsMycolic AcidsPeptidesPorA protein, Corynebacterium glutamicumPorins

Identifiers

PMID23852866
PMCPMC3754736
OpenAlexW2018769797

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.