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Identification of a c-type heme oxygenase and its function during acclimation of cyanobacteria to nitrogen fluctuations

ABSTRACT: Identification of a c-type heme oxygenase and its function during acclimation of cyanobacteria to nitrogen fluctuations

PROVIDER: PRJNA1007730 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR25714331_1.fastq.gz	Fastqsanger.gz
	SRR25714331_2.fastq.gz	Fastqsanger.gz
	SRR25714332_1.fastq.gz	Fastqsanger.gz
	SRR25714332_2.fastq.gz	Fastqsanger.gz
	SRR25714333_1.fastq.gz	Fastqsanger.gz

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Identification of a c-type heme oxygenase and its function during acclimation of cyanobacteria to nitrogen fluctuations

Project description:The mechanisms of acclimating to a nitrogen-fluctuating environment are necessary for the survival of aquatic cyanobacteria in their natural habitats, but our understanding is still far from complete. Here, the synthesis of phycobiliprotein is confirmed to be much earlier than that of photosystem components during recovery from nitrogen chlorosis and an unknown protein Ssr1698 is discovered to be involved in this synthetic process. The unknown protein is further identified as a c-type heme oxygenase (cHO) in tetrapyrrole biosynthetic pathway and catalyzes the opening of heme ring to form biliverdin IXα, which is required for phycobilin production and ensuing phycobiliprotein synthesis. In addition, the cHO-dependent phycobiliprotein is found to be vital for the growth of cyanobacterial cells during chlorosis and regreening through its nitrogen-storage and light-harvesting functions, respectively. Collectively, the cHO expressed preferentially during recovery from nitrogen chlorosis is identified in photosynthetic organisms and the dual function of this enzyme-dependent phycobiliprotein is proposed to be an important mechanism for acclimation of aquatic cyanobacteria to a nitrogen-fluctuating environment.

2023-08-24 | GSE241350 | GEO

Malaria parasites require a divergent heme oxygenase for apicoplast biogenesis

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Identification of a c-type heme oxygenase and its function during acclimation of cyanobacteria to nitrogen fluctuations.

| S-EPMC10504260 | biostudies-literature

Control of Renal Central Carbon Metabolism by Heme Oxygenase-1

Project description:Metabolic adaptation refers to the regulation of cellular metabolism to prevent tissue dysfunction in response to different forms of stress. Heme, an iron-containing porphyrin, is indispensable for oxygen transport and for the activity of hemoproteins such as catalases. Cytotoxic “labile” heme is readily degraded by two distinct heme oxygenases (HO). The conditional deletion of Hmox-1, the gene encoding the inducible heme-degrading enzyme heme oxygenase (HO)-1, impairs metabolic adaptation to malaria and to polymicrobial infection. Embryonic deficiency in HO-1 is partially lethal in mice and surviving animals show progressive chronic inflammatory disease making them an unsuitable model to study metabolic adaptation. Here we found that mice with an inducible deletion of Hmox1 (Hmox1R26Δ/Δ) but not control mice rapidly succumbed to sterile hemolytic stress. Mortality was associated with heme-driven kidney failure, hypoglycemia, and disruption of adaptive thermoregulation. RNA sequencing and targeted metabolomics combined with data-driven in silico metabolic modeling revealed that failed renal metabolic adaptation is driven by altered oxidative phosphorylation and impaired pentose phosphate pathway. Heme-induced kidney failure and mortality in Hmox1R26Δ/Δ mice was not prevented with impairment of the inflammatory response, nor with antioxidants. Our results emphasize the critical importance of Hmox1 expression in hemolytic stress leading to acute kidney injury and death.

2025-12-02 | GSE246570 | GEO

Heme oxygenase-1 knocked down rat mesangial cells treated with hydrogen peroxide

Project description:HO-1 cells denote the cultured rat mesangial cells with heme oxygenase-1 knocked down by RNA interference (using lentiviral vector). GFP cells denote the cultured rat mesangial cells that are transfected with empty lentiviral vector containing GFP cassette. Cells are treated with hydrogen peroxide 100 micromolar for 2 hours, or without. RNA are then harvested for array analysis. Biological replicates are performed (two independent experiment sets). GFP cell and HO-1 cell are untreated, or treated with hydrogen peroxide (100 micromolar for 2 hours).

2014-01-10 | E-GEOD-53953 | biostudies-arrayexpress

The heme regulatory motifs of heme oxygenase-2 function to transfer heme to the catalytic site for degradation

Project description:Heme regulatory motifs (HRMs) are found in a variety of proteins that are involved in diverse biological functions. In the C-terminal tail region of human heme oxygenase-2 (HO2), there are two HRMs whose cysteines form a disulfide bond; when reduced, these cysteines are available to bind Fe3+-heme. Heme binding to the HRMs is independent of the HO2 catalytic active site in the core of the protein, where heme binds with high affinity and is degraded to biliverdin. Here, we describe the reversible, protein-mediated transfer of heme between the HRMs and the core of HO2. Using HDX-MS to monitor the dynamics of HO2 with and without Fe3+-heme bound to the HRMs and to the core, we detected conformational changes in the catalytic core only in one state of the catalytic cycle – when Fe3+-heme is bound to the HRMs and the core is in the apo state. The conformational changes detected are consistent with transfer of heme between binding sites. Indeed, Fe3+-heme bound to the HRMs is transferred to the apo-core upon either independently expressing the core and a construct spanning the HRM-containing tail or after single turnover of heme at the core. In addition, we observed transfer of heme from the core to the HRMs and equilibration of heme between the core and HRMs. We thus propose a Fe3+-heme transfer model in which heme bound to the HRMs is readily transferred to the catalytic site for degradation to facilitate turnover but can also equilibrate between the sites to maintain heme homeostasis.

2020-03-18 | PXD017538 | Pride

Heme oxygenase-1 knocked down rat mesangial cells treated with hydrogen peroxide

2014-01-10 | GSE53953 | GEO

Identification of Cytoprotective Small Molecule Inducers of Heme Oxygenase-1

Project description:Identification of Cytoprotective Small Molecule Inducers of Heme Oxygenase-1

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Control of Renal Central Carbon Metabolism by Heme Oxygenase-1

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Heme oxygenase-1 orchestrates the immunosuppressive program of tumor-associated macrophages

Project description:Heme oxygenase-1 orchestrates the immunosuppressive program of tumor-associated macrophages

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