Evidence map›Paper›PMID 27517714›Full record

ArticlePLoS genetics2016

The DUF59 Containing Protein SufT Is Involved in the Maturation of Iron-Sulfur (FeS) Proteins during Conditions of High FeS Cofactor Demand in Staphylococcus aureus.

Ameya A Mashruwala, Shiven Bhatt, Saroj Poudel, Eric S Boyd, Jeffrey M Boyd

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

33 citing papers in PubMed, 56 citations in OpenAlex.

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  5. Regulation of airway fumarate by host and pathogen promotesbioRxiv : the preprint server for biology · 2025
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  9. ThebioRxiv : the preprint server for biology · 2024
    Article
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  13. Review
  14. Review
  15. Article
  16. Article
  17. Frontiers in microbiology · 2021
    Article
  18. Article
  19. Article
  20. Fe-S cluster biogenesis by the bacterial Suf pathway.Biochimica et biophysica acta. Molecular cell research · 2020
    Review
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 3 institutions in 1 country.

Ameya A MashruwalaDepartment of Biochemistry and Microbiology, Rutgers University, New Brunswick, New Jersey, United States of America.ORCID 0000-0001-5583-4174
Shiven BhattDepartment of Biochemistry and Microbiology, Rutgers University, New Brunswick, New Jersey, United States of America.
Saroj PoudelDepartment of Microbiology and Immunology, Montana State University, Bozeman, Montana, United States of America.
Eric S BoydDepartment of Microbiology and Immunology, Montana State University, Bozeman, Montana, United States of America.
Jeffrey M BoydDepartment of Biochemistry and Microbiology, Rutgers University, New Brunswick, New Jersey, United States of America.
Rutgers, The State University of New Jersey · USMontana State University · USNASA Astrobiology Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins containing DUF59 domains have roles in iron-sulfur (FeS) cluster assembly and are widespread throughout Eukarya, Bacteria, and Archaea. However, the function(s) of this domain is unknown. Staphylococcus aureus SufT is composed solely of a DUF59 domain. We noted that sufT is often co-localized with sufBC, which encode for the Suf FeS cluster biosynthetic machinery. Phylogenetic analyses indicated that sufT was recruited to the suf operon, suggesting a role for SufT in FeS cluster assembly. A S. aureus ΔsufT mutant was defective in the assembly of FeS proteins. The DUF59 protein Rv1466 from Mycobacterium tuberculosis partially corrected the phenotypes of a ΔsufT mutant, consistent with a widespread role for DUF59 in FeS protein maturation. SufT was dispensable for FeS protein maturation during conditions that imposed a low cellular demand for FeS cluster assembly. In contrast, the role of SufT was maximal during conditions imposing a high demand for FeS cluster assembly. SufT was not involved in the repair of FeS clusters damaged by reactive oxygen species or in the physical protection of FeS clusters from oxidants. Nfu is a FeS cluster carrier and nfu displayed synergy with sufT. Furthermore, introduction of nfu upon a multicopy plasmid partially corrected the phenotypes of the ΔsufT mutant. Biofilm formation and exoprotein production are critical for S. aureus pathogenesis and vancomycin is a drug of last-resort to treat staphylococcal infections. Defective FeS protein maturation resulted in increased biofilm formation, decreased production of exoproteins, increased resistance to vancomycin, and the appearance of phenotypes consistent with vancomycin-intermediate resistant S. aureus. We propose that SufT, and by extension the DUF59 domain, is an accessory factor that functions in the maturation of FeS proteins. In S. aureus, the involvement of SufT is maximal during conditions of high demand for FeS proteins.

Indexed as

Bacterial ProteinsBiofilmsIronIron-Sulfur ProteinsMutant ProteinsMycobacterium tuberculosisPhylogenyProtein DomainsReactive Oxygen SpeciesStaphylococcal InfectionsStaphylococcus aureusVancomycinVancomycin ResistanceBacterial ProteinsIronIron-Sulfur ProteinsMutant ProteinsReactive Oxygen SpeciesVancomycin

Identifiers

PMID27517714
PMCPMC4982691
OpenAlexW2510809205

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Registered trials

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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.