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S-Adenosylmethionine (SAM) diet defines offspring epigenetic modification and intergenerational immune response.

ABSTRACT: At the beginning of the experiment, a concentration of 50μM was used The treatment of Caenorhabditis elegans with MS adenosylmethionine has been found to promote the natural immunity of nematodes and increase their survival rate in Pseudomonas aeruginosa. We found that this elevated immunity has an epigenetic phenomenon that can be inherited to its offspring. To further explore its molecular mechanism, we aim to investigate the gene expression differences between S-adenosylmethionine treatment and untreated, as well as the similarities and differences in gene expression between S-adenosylmethionine treatment and offspring

ORGANISM(S): Caenorhabditis elegans

PROVIDER: GSE262167 | GEO | 2025/11/14

REPOSITORIES: GEO

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Project description:A [4Fe-4S](+) cluster reduces a bound S-adenosylmethionine (SAM) molecule, cleaving it into methionine and a 5'-deoxyadenosyl radical (5'-dA(•)). This step initiates the varied chemistry catalyzed by each of the so-called radical SAM enzymes. The strongly oxidizing 5'-dA(•) is quenched by abstracting a H-atom from a target species. In some cases, this species is an exogenous molecule of substrate, for example, L-tyrosine in the [FeFe] hydrogenase maturase, HydG. In other cases, the target is a proteinaceous residue as in all the glycyl radical forming enzymes. The generation of this initial radical species and the subsequent chemistry involving downstream radical intermediates is meticulously controlled by the enzyme so as to prevent unwanted reactions. But the manner in which this control is exerted is unknown. Electron paramagnetic resonance (EPR) spectroscopy has proven to be a valuable tool used to gain insight into these mechanisms. In this Account, we summarize efforts to trap such radical intermediates in radical SAM enzymes and highlight four examples in which EPR spectroscopic results have shed significant light on the corresponding mechanism. For lysine 2,3-aminomutase, nearly each possible intermediate, from an analogue of the initial 5'-dA(•) to the product radical L-β-lysine, has been explored. A paramagnetic intermediate observed in biotin synthase is shown to involve an auxiliary [FeS] cluster whose bridging sulfide is a co-substrate for the final step in the biosynthesis of vitamin B7. In HydG, the L-tyrosine substrate is converted in unprecedented fashion to a 4-oxidobenzyl radical on the way to generating CO and CN(-) ligands for the [FeFe] cluster of hydrogenase. And finally, EPR has confirmed a mechanistic proposal for the antibiotic resistance protein Cfr, which methylates the unactivated sp(2)-hybridized C8-carbon of an adenosine base of 23S ribosomal RNA. These four systems provide just a brief survey of the ever-growing set of radical SAM enzymes. The diverse chemistries catalyzed by these enzymes make them an intriguing target for continuing study, and EPR spectroscopy, in particular, seems ideally placed to contribute to our understanding.

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S-Adenosylmethionine (SAM) diet defines offspring epigenetic modification and intergenerational immune response.

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