ArticleJournal of bacteriology2005
Shigella dysenteriae ShuS promotes utilization of heme as an iron source and protects against heme toxicity.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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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.
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.
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Who cites it
30 citing papers in PubMed, 69 citations in OpenAlex.
- Heme in Bacterial Pathogenesis and as an Antimicrobial Target.Chemical reviews · 2025Review
- A new member of the flavodoxin superfamily from Fusobacterium nucleatum that functions in heme trafficking and reduction of anaerobilin.The Journal of biological chemistry · 2023Article
- Innate Bacteriostatic Mechanisms Defend the Urinary Tract.Annual review of physiology · 2022Review
- Iron Transport and Metabolism in Escherichia, Shigella, and Salmonella.EcoSal Plus · 2021Article
- Clostridioides difficile Senses and Hijacks Host Heme for Incorporation into an Oxidative Stress Defense System.Cell host & microbe · 2020Article
- Comprehensive analysis of iron utilization by Mycobacterium tuberculosis.PLoS pathogens · 2020Article
- New Insight into the Mechanism of Anaerobic Heme Degradation.Biochemistry · 2019Article
- Handling heme: The mechanisms underlying the movement of heme within and between cells.Free radical biology & medicine · 2019Review
- Heme sensing and detoxification by HatRT contributes to pathogenesis during Clostridium difficile infection.PLoS pathogens · 2018Article
- Transcriptional and posttranscriptional regulation of Shigella shuT in response to host-associated iron availability and temperature.MicrobiologyOpen · 2017Article
- Heme Synthesis and Acquisition in Bacterial Pathogens.Journal of molecular biology · 2016Review
- The crimson conundrum: heme toxicity and tolerance in GAS.Frontiers in cellular and infection microbiology · 2014Article
- Crystal structure of the Pseudomonas aeruginosa cytoplasmic heme binding protein, Apo-PhuS.Journal of inorganic biochemistry · 2013Article
- Sequestration and scavenging of iron in infection.Infection and immunity · 2013Article
- The P. aeruginosa heme binding protein PhuS is a heme oxygenase titratable regulator of heme uptake.ACS chemical biology · 2013Article
- Pseudomonas aeruginosa adapts its iron uptake strategies in function of the type of infections.Frontiers in cellular and infection microbiology · 2013Review
- Role and regulation of heme iron acquisition in gram-negative pathogens.Frontiers in cellular and infection microbiology · 2013Review
- Iron, copper, zinc, and manganese transport and regulation in pathogenic Enterobacteria: correlations between strains, site of infection and the relative importance of the different metal transport systems for virulence.Frontiers in cellular and infection microbiology · 2013Review
- RNA-mediated thermoregulation of iron-acquisition genes in Shigella dysenteriae and pathogenic Escherichia coli.PloS one · 2013Article
- Metabolic flux of extracellular heme uptake in Pseudomonas aeruginosa is driven by the iron-regulated heme oxygenase (HemO).The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Shigella dysenteriae serotype 1, a major cause of bacillary dysentery in humans, can use heme as a source of iron. Genes for the transport of heme into the bacterial cell have been identified, but little is known about proteins that control the fate of the heme molecule after it has entered the cell. The shuS gene is located within the heme transport locus, downstream of the heme receptor gene shuA. ShuS is a heme binding protein, but its role in heme utilization is poorly understood. In this work, we report the construction of a chromosomal shuS mutant. The shuS mutant was defective in utilizing heme as an iron source. At low heme concentrations, the shuS mutant grew slowly and its growth was stimulated by either increasing the heme concentration or by providing extra copies of the heme receptor shuA on a plasmid. At intermediate heme concentrations, the growth of the shuS mutant was moderately impaired, and at high heme concentrations, shuS was required for growth on heme. The shuS mutant did not show increased sensitivity to hydrogen peroxide, even at high heme concentrations. ShuS was also required for optimal utilization of heme under microaerobic and anaerobic conditions. These data are consistent with the model in which ShuS binds heme in a soluble, nontoxic form and potentially transfers the heme from the transport proteins in the membrane to either heme-containing or heme-degrading proteins. ShuS did not appear to store heme for future use.
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Registered trials
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.