Evidence map›Paper›PMID 19940132›Full record

ArticleThe Journal of biological chemistry2010

Disulfide bond formation and cysteine exclusion in gram-positive bacteria.

Robert Daniels, Peter Mellroth, Andreas Bernsel, Fabrice Neiers, Staffan Normark, Gunnar von Heijne, Birgitta Henriques-Normark

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

54 citing papers in PubMed, 96 citations in OpenAlex.

  1. TMcin RiPP biosynthesis in the cellular membrane.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Review
  4. Disulphide bond-forming enzymes in clostridial species.Microbiology (Reading, England) · 2025
    Article
  5. Article
  6. Article
  7. A cryptic oxidoreductase safeguards oxidative protein folding inProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Article
  9. The biogenesis of β-lactamase enzymes.Microbiology (Reading, England) · 2022
    Review
  10. The putative role of gut microbiota in cancer: Cysteine is a pivotal coin.Frontiers in gastroenterology (Lausanne, Switzerland) · 2022
    Review
  11. Interplay between DsbA1, DsbA2 and C8J_1298 Periplasmic Oxidoreductases ofInternational journal of molecular sciences · 2021
    Article
  12. Article
  13. Article
  14. Article
  15. Cysteine Proteome Reveals Response to Endogenous Oxidative Stress inInternational journal of molecular sciences · 2021
    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

7 authors at 3 institutions in 1 country.

Robert DanielsDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, SE-171 77 Stockholm, Sweden.
Peter Mellroth
Andreas Bernsel
Fabrice Neiers
Staffan Normark
Gunnar von Heijne
Birgitta Henriques-Normark
Karolinska Institutet · SEStockholm University · SESwedish Institute · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Most secretion pathways in bacteria and eukaryotic cells are challenged by the requirement for their substrate proteins to mature after they traverse a membrane barrier and enter a reactive oxidizing environment. For Gram-positive bacteria, the mechanisms that protect their exported proteins from misoxidation during their post-translocation maturation are poorly understood. To address this, we separated numerous bacterial species according to their tolerance for oxygen and divided their proteomes based on the predicted subcellular localization of their proteins. We then applied a previously established computational approach that utilizes cysteine incorporation patterns in proteins as an indicator of enzymatic systems that may exist in each species. The Sec-dependent exported proteins from aerobic Gram-positive Actinobacteria were found to encode cysteines in an even-biased pattern indicative of a functional disulfide bond formation system. In contrast, aerobic Gram-positive Firmicutes favor the exclusion of cysteines from both their cytoplasmic proteins and their substantially longer exported proteins. Supporting these findings, we show that Firmicutes, but not Actinobacteria, tolerate growth in reductant. We further demonstrate that the actinobacterium Corynebacterium glutamicum possesses disulfide-bonded proteins and two dimeric Dsb-like enzymes that can efficiently catalyze the formation of disulfide bonds. Our results suggest that cysteine exclusion is an important adaptive strategy against the challenges presented by oxidative environments.

Indexed as

ActinobacteriaBacterial ProteinsCorynebacterium glutamicumCysteineCytoplasmDisulfidesElectrophoresis, Polyacrylamide GelGene Expression Regulation, BacterialGram-Positive BacteriaOxidation-ReductionOxygenProtein FoldingProtein TransportProteomeBacterial ProteinsCysteineDisulfidesOxygenProteome

Identifiers

PMID19940132
PMCPMC2823432
OpenAlexW2109068727

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.