AI Article Synopsis
- The 2-methylthio modification at A37 in tRNAs is essential for precise decoding and maintaining metabolic balance in mammals, yet how this modification is regulated is not well understood.
- New research reveals that cysteine hydropersulfide (CysSSH), a recently discovered reactive sulfur compound, plays a key role in facilitating this modification in cells.
- Disruption of CysSSH production leads to a decrease in ms modification, which negatively affects insulin secretion and glucose metabolism, highlighting its importance in cellular processes.
Article Abstract
The 2-methylthio (ms) modification at A37 of tRNAs is critical for accurate decoding, and contributes to metabolic homeostasis in mammals. However, the regulatory mechanism of ms modification remains largely unknown. Here, we report that cysteine hydropersulfide (CysSSH), a newly identified reactive sulfur species, is involved in ms modification in cells. The suppression of intracellular CysSSH production rapidly reduced ms modification, which was rescued by the application of an exogenous CysSSH donor. Using a unique and stable isotope-labeled CysSSH donor, we show that CysSSH was capable of specifically transferring its reactive sulfur atom to the cysteine residues of ms-modifying enzymes as well as ms modification. Furthermore, the suppression of CysSSH production impaired insulin secretion and caused glucose intolerance in both a pancreatic β-cell line and mouse model. These results demonstrate that intracellular CysSSH is a novel sulfur source for ms modification, and that it contributes to insulin secretion.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5224495 | PMC |
| http://dx.doi.org/10.1093/nar/gkw745 | DOI Listing |
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