Evidence map›Paper›PMID 21338420›Full record

ArticleMolecular microbiology2011

A novel two-gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis.

Natalia Martin, Quin H Christensen, María C Mansilla, John E Cronan, Diego de Mendoza

Open access · greenAbstract read
In one paragraph

Article in Molecular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed, 1 pooled it
2.8field-weighted citation impact, top 11% 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

37 citing papers in PubMed, 1 synthesis or guideline pooled it, 55 citations in OpenAlex.

  1. The Surfactin-Like Lipopeptides FromFrontiers in bioengineering and biotechnology · 2021
    Pooled it
  2. Article
  3. Fatty acid synthesis and utilization in gram-positive bacteria: insights fromMicrobiology and molecular biology reviews : MMBR · 2025
    Review
  4. Applied and environmental microbiology · 2024
    Article
  5. Lipoic acid attachment to proteins: stimulating new developments.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  6. Article
  7. Article
  8. Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Article
  10. DefiningThe Journal of biological chemistry · 2020
    Article
  11. Article
  12. Article
  13. Review
  14. Functional Identification and Structural Analysis of a New Lipoate Protein Ligase inFrontiers in cellular and infection microbiology · 2020
    Article
  15. Article
  16. Advances in synthesis of biotin and assembly of lipoic acid.Current opinion in chemical biology · 2018
    Review
  17. Protein moonlighting elucidates the essential human pathway catalyzing lipoic acid assembly on its cognate enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2018
    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

5 authors at 4 institutions in 2 countries.

Natalia MartinInstituto de Biología Molecular y Celular de Rosario (IBR-CONICET), Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Suipacha 531, 2000 Rosario, Argentina.
Quin H Christensen
María C Mansilla
John E Cronan
Diego de Mendoza
Consejo Nacional de Investigaciones Científicas y Técnicas · ARInstituto de Biología Molecular y Celular de Rosario · ARInterface (United States) · USNational University of Rosario · AR

Funding

GENETIC APPROACHES TO REGULATION OF LIPID METABOLISMR01AI015650 · NIAID · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI CRONAN, JOHN E. · 1985 to 2022
$12.0M
Training Program in Chemistry-Interface with BiologyT32GM070421 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI HERGENROTHER, PAUL · 2005 to 2019
$5.4M
GENETIC APPROACHES TO REGULATION OF LIPID METABOLISMR37AI015650 · NIAID · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI CRONAN, JOHN E. · 1994 to 2003
$1.8M
NIAID NIH HHS R01 AI015650NIAID NIH HHS R37 AI015650NIGMS NIH HHS 5 T32 GM070421NIGMS NIH HHS T32 GM070421
6 · The paper itself

Abstract

The Bacillus subtilis genome encodes three apparent lipoyl ligase homologues: yhfJ, yqhM and ywfL, which we have renamed lplJ, lipM and lipL respectively. We show that LplJ encodes the sole lipoyl ligase of this bacterium. Physiological and biochemical characterization of a ΔlipM strain showed that LipM is absolutely required for the endogenous lipoylation of all lipoate-dependent proteins, confirming its role as the B. subtilis octanoyltransferase. However, we also report that in contrast to Escherichia coli, B. subtilis requires a third protein for lipoic acid assembly, LipL. B. subtilis ΔlipL strains are unable to synthesize lipoic acid despite the presence of LipM and the sulphur insertion enzyme, LipA, which should suffice for lipoic acid biosynthesis based on the E. coli model. LipM is only required for the endogenous lipoylation pathway, whereas LipL also plays a role in lipoic acid scavenging. Expression of E. coli lipB allows growth of B. subtilisΔlipL or ΔlipM strains in the absence of supplements. In contrast, growth of an E. coliΔlipB strain can be complemented with lipM, but not lipL. These data together with those of the companion article provide evidence that LipM and LipL catalyse sequential reactions in a novel pathway for lipoic acid biosynthesis.

Indexed as

Genes, BacterialBacillus subtilisBacterial ProteinsBiosynthetic PathwaysEscherichia coliGene DeletionGenetic Complementation TestModels, BiologicalThioctic AcidBacterial ProteinsThioctic Acid

Identifiers

PMID21338420
PMCPMC3086205
OpenAlexW1922014200

What OpenQuestion holds

Textmetadata
LicenceTDM
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.