Abstract
We identified breast cancer-associated protein (BCA3) as a novel binding partner of Mason-Pfizer monkey virus (MPMV) protease (PR). The interaction was confirmed by co-immunoprecipitation and immunocolocalization of MPMV PR and BCA3. Full-length but not C-terminally truncated BCA3 was incorporated into MPMV virions. We ruled out the potential role of the G-patch domain, a glycine-rich domain located at the C terminus of MPMV PR, in BCA3 interaction and virion incorporation. Expression of BCA3 did not affect MPMV particle release and proteolytic processing; however, it slightly increased MPMV infectivity.
© 2014 The Authors.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adaptor Proteins, Signal Transducing / chemistry
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Adaptor Proteins, Signal Transducing / genetics
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Adaptor Proteins, Signal Transducing / metabolism*
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Amino Acid Sequence
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Animals
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Endopeptidases / chemistry
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Endopeptidases / genetics
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Endopeptidases / metabolism*
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Female
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HEK293 Cells
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Humans
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Mason-Pfizer monkey virus / enzymology*
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Mason-Pfizer monkey virus / genetics
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Molecular Sequence Data
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Nuclear Proteins / chemistry
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Nuclear Proteins / genetics
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Nuclear Proteins / metabolism*
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Protein Binding
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Protein Interaction Domains and Motifs
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Sequence Homology, Amino Acid
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Species Specificity
Substances
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AKIP1 protein, human
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Adaptor Proteins, Signal Transducing
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Nuclear Proteins
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Recombinant Proteins
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Endopeptidases
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Mason-Pfizer monkey virus protease