Evidence map›Paper›PMID 21965560›Full record

ArticleJournal of bacteriology2011

Deletion strains reveal metabolic roles for key elemental sulfur-responsive proteins in Pyrococcus furiosus.

Stephanie L Bridger, Sonya M Clarkson, Karen Stirrett, Megan B DeBarry, Gina L Lipscomb, Gerrit J Schut, Janet Westpheling, Robert A Scott, Michael W W Adams

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.9field-weighted citation impact, top 6% 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, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Metabolic Adaptation to Sulfur of HyperthermophilicInternational journal of molecular sciences · 2020
    Article
  8. Article
  9. Article
  10. Article
  11. Biotechnology of extremely thermophilic archaea.FEMS microbiology reviews · 2018
    Review
  12. Review
  13. Two functionally distinct NADPThe Journal of biological chemistry · 2017
    Article
  14. Physiological, metabolic and biotechnological features of extremely thermophilic microorganisms.Wiley interdisciplinary reviews. Systems biology and medicine · 2017
    Review
  15. Genomic Analysis ofFrontiers in microbiology · 2017
    Article
  16. Article
  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

9 authors at 1 institution in 1 country.

Stephanie L BridgerDepartment of Biochemistry and Molecular Biology, Life Sciences Bldg., University of Georgia, Athens, GA 30602-7229, USA.
Sonya M Clarkson
Karen Stirrett
Megan B DeBarry
Gina L Lipscomb
Gerrit J Schut
Janet Westpheling
Robert A Scott
Michael W W Adams
University of Georgia · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transcriptional and enzymatic analyses of Pyrococcus furiosus previously indicated that three proteins play key roles in the metabolism of elemental sulfur (S(0)): a membrane-bound oxidoreductase complex (MBX), a cytoplasmic coenzyme A-dependent NADPH sulfur oxidoreductase (NSR), and sulfur-induced protein A (SipA). Deletion strains, referred to as MBX1, NSR1, and SIP1, respectively, have now been constructed by homologous recombination utilizing the uracil auxotrophic COM1 parent strain (ΔpyrF). The growth of all three mutants on maltose was comparable without S(0), but in its presence, the growth of MBX1 was greatly impaired while the growth of NSR1 and SIP1 was largely unaffected. In the presence of S(0), MBX1 produced little, if any, sulfide but much more acetate (per unit of protein) than the parent strain, demonstrating that MBX plays a critical role in S(0) reduction and energy conservation. In contrast, comparable amounts of sulfide and acetate were produced by NSR1 and the parent strain, indicating that NSR is not essential for energy conservation during S(0) reduction. Differences in transcriptional responses to S(0) in NSR1 suggest that two sulfide dehydrogenase isoenzymes provide a compensatory NADPH-dependent S(0) reduction system. Genes controlled by the S(0)-responsive regulator SurR were not as highly regulated in MBX1 and NSR1. SIP1 produced the same amount of acetate but more sulfide than the parent strain. That SipA is not essential for growth on S(0) indicates that it is not required for detoxification of metal sulfides, as previously suggested. A model is proposed for S(0) reduction by P. furiosus with roles for MBX and NSR in bioenergetics and for SipA in iron-sulfur metabolism.

Indexed as

Sequence DeletionArchaeal ProteinsGene Expression Regulation, ArchaealMembrane ProteinsOxidation-ReductionOxidoreductasesPyrococcus furiosusSulfurArchaeal ProteinsMembrane ProteinsOxidoreductasesSipA protein, Pyrococcus furiosusSulfur

Identifiers

PMID21965560
PMCPMC3232869
OpenAlexW2103537475

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.