Characterization of glutathione-specific gamma glutamyl cyclotransferase (ChaC) in Bombyx mori
- PMID: 37283485
- DOI: 10.1002/arch.22027
Characterization of glutathione-specific gamma glutamyl cyclotransferase (ChaC) in Bombyx mori
Abstract
Glutathione (GSH) contributes to redox maintenance and detoxification of various xenobiotic and endogenous substances. γ-glutamyl cyclotransferase (ChaC) is involved in GSH degradation. However, the molecular mechanism underlying GSH degradation in silkworms (Bombyx mori) remains unknown. Silkworms are lepidopteran insects that are considered to be an agricultural pest model. We aimed to examine the metabolic mechanism underlying GSH degradation mediated by B. mori ChaC and successfully identified a novel ChaC gene in silkworms (herein, bmChaC). The amino acid sequence and phylogenetic tree revealed that bmChaC was closely related to mammalian ChaC2. We overexpressed recombinant bmChaC in Escherichia coli, and the purified bmChaC showed specific activity toward GSH. Additionally, we examined the degradation of GSH to 5-oxoproline and cysteinyl glycine via liquid chromatography-tandem mass spectrometry. Quantitative real-time polymerase chain reaction revealed that bmChaC mRNA expression was observed in various tissues. Our results suggest that bmChaC participates in tissue protection via GSH homeostasis. This study provides new insights into the activities of ChaC and the underlying molecular mechanisms that can aid the development of insecticides to control agricultural pests.
Keywords: 5-oxoproline; Bombyx mori; glutathione; reactive oxygen species; γ-glutamyl cyclotransferase.
© 2023 Wiley Periodicals LLC.
Similar articles
-
Characterization of a glutamate-cysteine ligase in Bombyx mori.Mol Biol Rep. 2023 Mar;50(3):2623-2631. doi: 10.1007/s11033-022-08191-6. Epub 2023 Jan 13. Mol Biol Rep. 2023. PMID: 36637620
-
A γ-glutamyl cyclotransferase protects Arabidopsis plants from heavy metal toxicity by recycling glutamate to maintain glutathione homeostasis.Plant Cell. 2013 Nov;25(11):4580-95. doi: 10.1105/tpc.113.111815. Epub 2013 Nov 8. Plant Cell. 2013. PMID: 24214398 Free PMC article.
-
Glutathione and glutathione-dependent enzymes: From biochemistry to gerontology and successful aging.Ageing Res Rev. 2023 Dec;92:102066. doi: 10.1016/j.arr.2023.102066. Epub 2023 Sep 7. Ageing Res Rev. 2023. PMID: 37683986 Review.
-
A gamma-glutamyl transpeptidase-independent pathway of glutathione catabolism to glutamate via 5-oxoproline in Arabidopsis.Plant Physiol. 2008 Nov;148(3):1603-13. doi: 10.1104/pp.108.125716. Epub 2008 Sep 3. Plant Physiol. 2008. PMID: 18768907 Free PMC article.
-
Degradation of glutathione and glutathione conjugates in plants.J Exp Bot. 2023 Jun 6;74(11):3313-3327. doi: 10.1093/jxb/erad018. J Exp Bot. 2023. PMID: 36651789 Review.
References
REFERENCES
-
- Abbott, J.J., Pei, J., Ford, J.L., Qi, Y., Grishin, V.N., Pitcher, L.A. et al. (2001) Structure prediction and active site analysis of the metal binding determinants in γ-glutamylcysteine synthetase. Journal of Biological Chemistry, 276(45), 42099-42107. https://doi.org/10.1074/jbc.M104672200
-
- Afrin, W., Furuya, S. & Yamamoto, K. (2023) Characterization of a glutamate-cysteine ligase in Bombyx mori. Molecular Biology Reports, 50(3), 2623-2631. https://doi.org/10.1007/s11033-022-08191-6
-
- Fahey, R.C., Newton, G.L., Arrick, B., Overdank-Bogart, T. & Aley, S.B. (1984) Entamoeba histolytica: a eukaryote without glutathione metabolism. Science, 224(4644), 70-72. https://doi.org/10.1126/science.6322306
-
- Franco, R. & Cidlowski, J.A. (2009) Apoptosis and glutathione: beyond an antioxidant. Cell Death & Differentiation, 16(10), 1303-1314. https://doi.org/10.1038/cdd.2009.107
-
- Ganguli, D., Kumar, C. & Bachhawat, A.K. (2007) The alternative pathway of glutathione degradation is mediated by a novel protein complex involving three new genes in Saccharomyces cerevisiae. Genetics, 175(3), 1137-1151. https://doi.org/10.1534/genetics.106.066944
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources