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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2000-5-31
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pubmed:abstractText |
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).
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Erythroid-Specific DNA-Binding...,
http://linkedlifedata.com/resource/pubmed/chemical/Fad7 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acid Desaturases,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Reactive Oxygen Species,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Thioredoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0950-382X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
35
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1540-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10760153-Amino Acid Substitution,
pubmed-meshheading:10760153-Animals,
pubmed-meshheading:10760153-Apoptosis,
pubmed-meshheading:10760153-Arabidopsis Proteins,
pubmed-meshheading:10760153-DNA Damage,
pubmed-meshheading:10760153-DNA-Binding Proteins,
pubmed-meshheading:10760153-Erythroid-Specific DNA-Binding Factors,
pubmed-meshheading:10760153-Escherichia coli,
pubmed-meshheading:10760153-Fatty Acid Desaturases,
pubmed-meshheading:10760153-Genes, Lethal,
pubmed-meshheading:10760153-Mammals,
pubmed-meshheading:10760153-Mutation,
pubmed-meshheading:10760153-Oxygen,
pubmed-meshheading:10760153-Peptide Fragments,
pubmed-meshheading:10760153-Protein Conformation,
pubmed-meshheading:10760153-Reactive Oxygen Species,
pubmed-meshheading:10760153-Recombinant Proteins,
pubmed-meshheading:10760153-Suppression, Genetic,
pubmed-meshheading:10760153-Thioredoxins,
pubmed-meshheading:10760153-Transcription Factors
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pubmed:year |
2000
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pubmed:articleTitle |
Death effector domain of a mammalian apoptosis mediator, FADD, induces bacterial cell death.
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pubmed:affiliation |
National Creative Research Initiatives Centre for ARS Network, Sung Kyun Kwan University, 300 Chunchundong, Jangangu, Suwon, Kyunggido 44-746, Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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