Abstract
By co-immunoprecipitation analysis, we demonstrated that wt-p53 formed a complex with non-structural protein (NS) 3 of hepatitis C virus, both in the absence and the presence of NS4A, a viral cofactor that strongly associates with NS3. Deletional analysis revealed that a portion near the N-terminus of NS3 (amino acids (aa) 1055 and 1200), which is different from the NS4A binding site, was necessary for the complex formation with wt-p53. On the other hand, a portion near the C-terminus of wt-p53 (aa 301-360), which has been reported to contain the oligomerization domain, was important for the complex formation with NS3.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Base Sequence
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DNA Primers
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HeLa Cells
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Hepacivirus / metabolism*
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Humans
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Molecular Sequence Data
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Recombinant Proteins / chemistry
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Sequence Deletion
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Transfection
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Tumor Suppressor Protein p53 / chemistry
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Tumor Suppressor Protein p53 / isolation & purification
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Tumor Suppressor Protein p53 / metabolism*
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Viral Nonstructural Proteins / chemistry
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Viral Nonstructural Proteins / genetics
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Viral Nonstructural Proteins / metabolism*
Substances
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DNA Primers
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NS3 protein, hepatitis C virus
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NS4 protein, hepatitis C virus
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Recombinant Proteins
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Tumor Suppressor Protein p53
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Viral Nonstructural Proteins