Document Detail


Death effector domain of a mammalian apoptosis mediator, FADD, induces bacterial cell death.
MedLine Citation:
PMID:  10760153     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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).
Authors:
S W Lee; Y G Ko; S Bang; K S Kim; S Kim
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Molecular microbiology     Volume:  35     ISSN:  0950-382X     ISO Abbreviation:  Mol. Microbiol.     Publication Date:  2000 Mar 
Date Detail:
Created Date:  2000-05-31     Completed Date:  2000-05-31     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  8712028     Medline TA:  Mol Microbiol     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  1540-9     Citation Subset:  IM    
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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MeSH Terms
Descriptor/Qualifier:
Amino Acid Substitution
Animals
Apoptosis
Arabidopsis Proteins*
DNA Damage / genetics
DNA-Binding Proteins / genetics,  metabolism
Erythroid-Specific DNA-Binding Factors
Escherichia coli / genetics*
Fatty Acid Desaturases / chemistry,  genetics*,  metabolism*
Genes, Lethal
Mammals
Mutation
Oxygen / metabolism
Peptide Fragments / genetics,  metabolism
Protein Conformation
Reactive Oxygen Species
Recombinant Proteins / genetics,  metabolism
Suppression, Genetic
Thioredoxins / genetics,  metabolism
Transcription Factors / genetics,  metabolism
Chemical
Reg. No./Substance:
0/Arabidopsis Proteins; 0/DNA-Binding Proteins; 0/Erythroid-Specific DNA-Binding Factors; 0/Peptide Fragments; 0/Reactive Oxygen Species; 0/Recombinant Proteins; 0/Transcription Factors; 52500-60-4/Thioredoxins; 7782-44-7/Oxygen; EC 1.14.19.-/Fatty Acid Desaturases; EC 1.14.99.-/Fad7 protein, Arabidopsis

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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