Molecular mechanisms of lifespan extension in long-lived mitocondrial superoxide dismutase sod-2 mutants
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ABSTRACT:
PROVIDER: PRJNA1208437 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR31940225_1.fastq.gz | Fastqsanger.gz | |||
| SRR31940225_2.fastq.gz | Fastqsanger.gz | |||
| SRR31940226_1.fastq.gz | Fastqsanger.gz | |||
| SRR31940226_2.fastq.gz | Fastqsanger.gz | |||
| SRR31940227_1.fastq.gz | Fastqsanger.gz |
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Project description:To explore the molecular mechanisms of lifespan extension in sod-2 mutants in an unbiased manner, we used RNA sequencing to identify differentially expressed genes in sod-2 mutants compared to wild-type worms. We found a large number of gene expression changes at day 1 of adulthood and much fewer at day 8. Upregulated genes in sod-2 mutants included genes involved in innate immunity and cuticle development. There were many more differentially expressed genes between day 1 and day 8 of adulthood compared to differences between the genotypes.
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Project description:Enterocyte Superoxide Dismutase 2 Deletion Drives Hyperinsulinemia and Obesity
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Project description:The proteins are a pair of closely related superoxide dismutase (SOD) enzymes from the Gram positive bacterium, Staphylococcus aureus. SodA is a Mn-specific SOD (MnSOD), which is inactive when loaded with Fe, whereas SodM is a 'cambialistic' SOD (camSOD), which is catalytically active with either Mn or Fe as a cofactor. Their sequences are 75% identical across their 199 amino acid sequences: the crystal structures of each enzyme in each metal-loaded form: Mn-loaded MnSOD SodA: PDB ID 5N56 Fe-loaded MnSOD SodA: PDB ID 6EX3 Mn-loaded camSOD SodM: PDB ID 5N57 Fe-loaded camSOD SodM: PDB ID 6EX4 The resulting structures (all to approximately 2A resolution) showed no significant differences that indicated molecular reasons for the differences in activity. Because of the differences in activity, therefore, the project aimed to compare three forms of these enzymes to determine whether there are any differences in the dynamics of regions of their structure, most notably those within the active site and the putative substrate access route(s).
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Project description:Defenses against oxidants are crucial for the virulence of pathogens, with superoxide scavenging enzymes (SOSEs) playing a vital role for most aerobes. However, our knowledge of superoxide adaptation primarily stems from the study of SOSE-encoding bacteria. Here, we investigated the evolution of a naturally SOSE-deficient pathogen (Leptospira spp.), along with the alternative mechanisms it recruits to combat superoxide stress. We demonstrate that emergence of pathogenic Leptospira correlated with SOD loss, but that a long-lasting adaptation to superoxide remains possible. We reveal that cysteine and leucine biosynthesis are the most induced pathways in response to superoxide and demonstrate the importance of sulfur metabolism in superoxide adaptation in this SOSE-deficient model. We also propose cysteine oxidation as a key mediator of superoxide toxicity in the absence of SOSEs. This study challenges our conventional understanding of the oxygen toxicity theory and proposes a new model of superoxide adaptation through metabolic rewiring in bacteria.
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