Lee, SW Ko, YG Bang, S Kim, KS Kim, S 2024-01-21T14:13:52Z 2024-01-21T14:13:52Z 2021-09-05 2000-03 0950-382X https://pubs.kist.re.kr/handle/201004/141537 FADD is a mammalian pro-apoptotic mediator consisting of the N-terminal death effector domain (DED) and the C-terminal death domain (DD). The N-terminal 88-residue fragment of murine FADD was defined as the stable structural unit of DED, as determined by proteolytic digestion and conformational analysis. This domain induced bacterial as well as mammalian cell death, whereas the full-length or DD of FADD did not. The Escherichia coli cells expressing FADD-DED showed elongated cell morphology and an increased level of nicked chromosomal DNA and mutation. The lethality of FADD-DED was abolished by co-expression of thioredoxin and superoxide dismutase or relieved by the addition of vitamin E as a reducing agent and under anaerobic growth conditions. The toxicity of FADD-DED was genetically suppressed by various oxidoreductases of E. coli. All these results suggest that the death effector domain of mammalian FADD induced bacterial cell death by enhancing cellular levels of reactive oxygen species (ROS). English WILEY Death effector domain of a mammalian apoptosis mediator, FADD, induces bacterial cell death Article 10.1046/j.1365-2958.2000.01824.x 1 MOLECULAR MICROBIOLOGY, v.35, no.6, pp.1540 - 1549 MOLECULAR MICROBIOLOGY 35 6 1540 1549 N scie scopus 000086011100024 2-s2.0-0034067779 Biochemistry & Molecular Biology Microbiology Biochemistry & Molecular Biology Microbiology Article ESCHERICHIA-COLI SUPEROXIDE-DISMUTASE HYDROGEN-PEROXIDE SIGNALING COMPLEX CD95 FAS/APO-1 NMR STRUCTURE THIOREDOXIN FAS PROTEIN DAMAGE FADD apoptosis death effector domain death domain