ArticleThe Journal of biological chemistry2010
The 2-Cys peroxiredoxin alkyl hydroperoxide reductase c binds heme and participates in its intracellular availability in Streptococcus agalactiae.
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 25 papers.
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25 citing papers in PubMed, 47 citations in OpenAlex.
- Oxidative stress modulates heme synthesis and induces peroxiredoxin-2 as a novel cytoprotective response in β-thalassemic erythropoiesis.Haematologica · 2011Trial
- Virulence characteristics of Gram-positive bacteria isolated from diabetic foot ulcers.FEMS microbes · 2024Article
- Studying the Human Microbiota: Advances in Understanding the Fundamentals, Origin, and Evolution of Biological Timekeeping.International journal of molecular sciences · 2023Review
- The Role of Regulator Catabolite Control Protein A (CcpA) in Streptococcus agalactiae Physiology and Stress Response.Microbiology spectrum · 2022Article
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- Sequence characterisation and novel insights into bovine mastitis-associated Streptococcus uberis in dairy herds.Scientific reports · 2021Article
- Article
- Glutathione Synthesis Contributes to Virulence ofJournal of bacteriology · 2019Article
- Exoproteome Heterogeneity among Closely Related Staphylococcus aureus t437 Isolates and Possible Implications for Virulence.Journal of proteome research · 2019Article
- Intracellular proteins moonlighting as bacterial adhesion factors.AIMS microbiology · 2018Review
- Adaptation to Aerobic Environment ofFrontiers in microbiology · 2018Article
- Peroxiredoxin 1 (Prx1) is a dual-function enzyme by possessing Cys-independent catalase-like activity.The Biochemical journal · 2017Article
- Acid Stress Response Mechanisms of Group B Streptococci.Frontiers in cellular and infection microbiology · 2017Review
- Mitochondrial Cytochrome c Oxidase Biogenesis Is Regulated by the Redox State of a Heme-Binding Translational Activator.Antioxidants & redox signaling · 2016Article
- Characterization of two Lactococcus lactis zinc membrane proteins, Llmg_0524 and Llmg_0526, and role of Llmg_0524 in cell wall integrity.BMC microbiology · 2015Article
- Cysteine-independent Catalase-like Activity of Vertebrate Peroxiredoxin 1 (Prx1).The Journal of biological chemistry · 2015Article
- The MF6p/FhHDM-1 major antigen secreted by the trematode parasite Fasciola hepatica is a heme-binding protein.The Journal of biological chemistry · 2014Article
- The crimson conundrum: heme toxicity and tolerance in GAS.Frontiers in cellular and infection microbiology · 2014Article
- Protein expression and transcription profiles of three strains of Aeromonas salmonicida ssp. salmonicida under normal and iron-limited culture conditions.Proteome science · 2014Article
- A heme-sensing mechanism in the translational regulation of mitochondrial cytochrome c oxidase biogenesis.Cell metabolism · 2012Article
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7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heme is a redox-reactive molecule with vital and complex roles in bacterial metabolism, survival, and virulence. However, few intracellular heme partners were identified to date and are not well conserved in bacteria. The opportunistic pathogen Streptococcus agalactiae (group B Streptococcus) is a heme auxotroph, which acquires exogenous heme to activate an aerobic respiratory chain. We identified the alkyl hydroperoxide reductase AhpC, a member of the highly conserved thiol-dependent 2-Cys peroxiredoxins, as a heme-binding protein. AhpC binds hemin with a K(d) of 0.5 microm and a 1:1 stoichiometry. Mutagenesis of cysteines revealed that hemin binding is dissociable from catalytic activity and multimerization. AhpC reductase activity was unchanged upon interaction with heme in vitro and in vivo. A group B Streptococcus ahpC mutant displayed attenuation of two heme-dependent functions, respiration and activity of a heterologous catalase, suggesting a role for AhpC in heme intracellular fate. In support of this hypothesis, AhpC-bound hemin was protected from chemical degradation in vitro. Our results reveal for the first time a role for AhpC as a heme-binding protein.
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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.