The NAD+ -dependent deacetylase, Bifidobacterium longum Sir2 in response to oxidative stress by deacetylating SigH (σH ) and FOXO3a in Bifidobacterium longum and HEK293T cell respectively

Free Radical Biology & Medicine
Qing GuoYan Yang

Abstract

Silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation. The mammalian sirtuin family SIRT1, SIRT2, SIRT3 and SIRT6 can regulate oxidative stress. The probiotics (Bifidobacterium longum(B.longum) and Lactobacillus acidophilus(L. acidophilus)) have Sir2 gene family and have antioxidant activity in human body. it remains unknown whether probiotics Sir2 has a direct role in regulating oxidative stress. To this end, we knockout BL-sir2(sir2 B. longum) and LA-sir2(sir2 L.acidophilus) in low oxygen level. The antioxidant activities of two sir2 deficient strains was decreased, while when reintroduction of BL-sir2 and LA-sir2, the antioxidant activities were recoveried. In order to understand the regulation mechanism of probiotics Sir2 oxidation response. Then, we screened 65 acetylated protein, and found that SigH (σH) was a substrate of BL-Sir2. In addition, the acetylation level of σH decreased with the increase of BL-Sir2 level in B. longum. Thus, BL-Sir2 deacetylated σH in response to oxidative stress. Next, we transfected BL-Sir2 into H2O2-induced oxidative damage of 293T cells, BL-Sir2 increased the activity of manganese superoxide dismutase (MnSOD/SOD2) and catalase (CAT) and re...Continue Reading

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Citations

Dec 18, 2020·Comprehensive Reviews in Food Science and Food Safety·Mustapha MbyeMutamed M Ayyash
Aug 3, 2021·Journal of Immunology Research·Shunyu YaoXiaolu Liu

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