Abstract
We report here the purification and cDNA cloning of Apaf-1, a novel 130 kd protein from HeLa cell cytosol that participates in the cytochrome c-dependent activation of caspase-3. The NH2-terminal 85 amino acids of Apaf-1 show 21% identity and 53% similarity to the NH2-terminal prodomain of the Caenorhabditis elegans caspase, CED-3. This is followed by 320 amino acids that show 22% identity and 48% similarity to CED-4, a protein that is believed to initiate apoptosis in C. elegans. The COOH-terminal region of Apaf-1 comprises multiple WD repeats, which are proposed to mediate protein-protein interactions. Cytochrome c binds to Apaf-1, an event that may trigger the activation of caspase-3, leading to apoptosis.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Apoptotic Protease-Activating Factor 1
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Caenorhabditis elegans / metabolism
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Caenorhabditis elegans Proteins*
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Calcium-Binding Proteins / metabolism
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Caspase 3
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Caspases*
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Cell Line
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Cloning, Molecular
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Cysteine Endopeptidases / biosynthesis
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Cysteine Endopeptidases / metabolism*
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Cytochrome c Group / metabolism*
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Cytosol / metabolism
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DNA, Complementary
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Enzyme Activation
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Enzyme Precursors / metabolism
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HeLa Cells
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Helminth Proteins / metabolism
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Humans
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Molecular Sequence Data
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Proteins / chemistry*
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Proteins / isolation & purification
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Proteins / metabolism*
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Sequence Alignment
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Sequence Homology, Amino Acid
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Transfection
Substances
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APAF1 protein, human
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Apoptotic Protease-Activating Factor 1
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Caenorhabditis elegans Proteins
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Calcium-Binding Proteins
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Ced-4 protein, C elegans
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Cytochrome c Group
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DNA, Complementary
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Enzyme Precursors
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Helminth Proteins
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Proteins
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Recombinant Proteins
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CASP3 protein, human
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Caspase 3
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Caspases
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Cysteine Endopeptidases