Evidence map›Paper›PMID 25318663›Full record

ArticleMolecular microbiology2014

The CsoR-like sulfurtransferase repressor (CstR) is a persulfide sensor in Staphylococcus aureus.

Justin L Luebke, Jiangchuan Shen, Kevin E Bruce, Thomas E Kehl-Fie, Hui Peng, Eric P Skaar, David P Giedroc

Open access · greenAbstract read
In one paragraph

Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
4.5field-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

74 citing papers in PubMed, 115 citations in OpenAlex.

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14 more citing papers are in PubMed but not listed here.

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.

Justin L LuebkeDepartment of Chemistry, Indiana University, Bloomington, IN, 47405-7102, USA.
Jiangchuan Shen
Kevin E Bruce
Thomas E Kehl-Fie
Hui Peng
Eric P Skaar
David P Giedroc
Indiana University Bloomington · USUniversity of Illinois Urbana-Champaign · USVanderbilt University · US

Funding

Mechanism and function of heme-iron utilization in staphylococcal pathogenesisR01AI069233 · NIAID · VANDERBILT UNIVERSITY MEDICAL CENTER · PI SKAAR, ERIC P · 2006 to 2020
$5.6M
New mechanisms of sulfur sensing and trafficking in Staphylococcus aureus.R01GM097225 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI GIEDROC, DAVID P. · 2011 to 2014
$1.1M
Adaptation of Staphylococcus aureus to Mn and Zn starvation imposed by the hostK22AI104805 · NIAID · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI KEHL-FIE, THOMAS EVERETT · 2014 to 2015
$264k
Adaptation of Staphylococcus aureus to Mn-limitation imposed by the hostF32AI100480 · NIAID · VANDERBILT UNIVERSITY · PI KEHL-FIE, THOMAS EVERETT · 2012 to 2013
$78k
NIAID NIH HHS F32 AI100480NIAID NIH HHS K22 AI104805NIAID NIH HHS R01 AI069233NIGMS NIH HHS R01 GM097225
6 · The paper itself

Abstract

How cells regulate the bioavailability of utilizable sulfur while mitigating the effects of hydrogen sulfide toxicity is poorly understood. CstR [Copper-sensing operon repressor (CsoR)-like sulfurtransferase repressor] represses the expression of the cst operon encoding a putative sulfide oxidation system in Staphylococcus aureus. Here, we show that the cst operon is strongly and transiently induced by cellular sulfide stress in an acute phase and specific response and that cst-encoded genes are necessary to mitigate the effects of sulfide toxicity. Growth defects are most pronounced when S. aureus is cultured in chemically defined media with thiosulfate (TS) as a sole sulfur source, but are also apparent when cystine is used or in rich media. Under TS growth conditions, cells fail to grow as a result of either unregulated expression of the cst operon in a ΔcstR strain or transformation with a non-inducible C31A/C60A CstR that blocks cst induction. This suggests that the cst operon contributes to cellular sulfide homeostasis. Tandem high-resolution mass spectrometry reveals derivatization of CstR by both inorganic tetrasulfide and an organic persulfide, glutathione persulfide, to yield a mixture of Cys31-Cys60' interprotomer cross-links, including di-, tri- and tetrasulfide bonds, which allosterically inhibit cst operator DNA binding by CstR.

Indexed as

Bacterial ProteinsCopperCulture MediaGene Expression Regulation, BacterialHydrogen SulfideOperonRepressor ProteinsStaphylococcus aureusSulfidesTandem Mass SpectrometryBacterial ProteinsCopperCulture MediaHydrogen SulfidepersulfidesRepressor ProteinsSulfides

Identifiers

PMID25318663
PMCPMC4264537
OpenAlexW1496897103

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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.