Breast cancer-associated protein--a novel binding partner of Mason-Pfizer monkey virus protease
Language English Country England, Great Britain Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Adaptor Proteins, Signal Transducing chemistry genetics metabolism MeSH
- Species Specificity MeSH
- Endopeptidases chemistry genetics metabolism MeSH
- HEK293 Cells MeSH
- Protein Interaction Domains and Motifs MeSH
- Nuclear Proteins chemistry genetics metabolism MeSH
- Humans MeSH
- Mason-Pfizer monkey virus enzymology genetics MeSH
- Molecular Sequence Data MeSH
- Recombinant Proteins chemistry genetics metabolism MeSH
- Amino Acid Sequence MeSH
- Sequence Homology, Amino Acid MeSH
- Protein Binding MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Female MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Adaptor Proteins, Signal Transducing MeSH
- AKIP1 protein, human MeSH Browser
- Endopeptidases MeSH
- Nuclear Proteins MeSH
- Mason-Pfizer monkey virus protease MeSH Browser
- Recombinant Proteins MeSH
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.
References provided by Crossref.org
Unveiling the DHX15-G-patch interplay in retroviral RNA packaging
