Abstract
Human Bfl-1 is an anti-apoptotic Bcl-2 family member. Here, we found that Bfl-1 was converted into a potent death-promoting protein by green fluorescent protein (GFP) fusion with its N-terminus. The transient expression of GFP-Bfl-1 induced cytochrome c release and triggered apoptosis in 293T cells, which depended on the mitochondrial localization of GFP-Bfl-1. Apoptosis induced by GFP-Bfl-1 was significantly blocked by the pan-caspase inhibitor carbobenzoxy-Val-Ala-Asp-fluoromethyl ketone, but was not blocked by either Bcl-xL or Bfl-1. Our findings provide a useful model for understanding the structural basis of Bcl-2 family proteins that act in an opposite way despite sharing structural similarity between anti-apoptotic and pro-apoptotic proteins.
MeSH terms
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Apoptosis*
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Caspases / physiology
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Cell Line
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Cytochrome c Group / metabolism
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Green Fluorescent Proteins
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Humans
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Luminescent Proteins / genetics
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Minor Histocompatibility Antigens
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Mitochondria / chemistry
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Mitochondria / metabolism
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Protein Structure, Tertiary
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Proto-Oncogene Proteins c-bcl-2 / chemistry*
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Proto-Oncogene Proteins c-bcl-2 / genetics
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Proto-Oncogene Proteins c-bcl-2 / metabolism
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Recombinant Fusion Proteins / analysis
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Recombinant Fusion Proteins / antagonists & inhibitors
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Recombinant Fusion Proteins / metabolism
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bcl-X Protein
Substances
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BCL2-related protein A1
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BCL2L1 protein, human
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Cytochrome c Group
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Luminescent Proteins
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Minor Histocompatibility Antigens
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Proto-Oncogene Proteins c-bcl-2
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Recombinant Fusion Proteins
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bcl-X Protein
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Green Fluorescent Proteins
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Caspases