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One-step separation of myristoylated and nonmyristoylated retroviral matrix proteins
M. Doležal, A. Zábranský, R. Hrabal, T. Ruml, I. Pichová, M. Rumlová,
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- chromatografie afinitní MeSH
- klonování DNA MeSH
- kyselina myristová chemie metabolismus MeSH
- myši MeSH
- nukleární magnetická rezonance biomolekulární MeSH
- rekombinantní proteiny chemie genetika izolace a purifikace metabolismus MeSH
- Retroviridae - proteiny chemie genetika izolace a purifikace metabolismus MeSH
- retrovirové infekce virologie MeSH
- virus myší leukemie chemie genetika metabolismus MeSH
- zvířata MeSH
- Check Tag
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
N-terminal myristoylation of retroviral matrix proteins is essential for the targeting of the Gag polyproteins to the plasma membrane. To investigate the effect of the myristoylation on the structure and membrane binding ability of the matrix proteins, it is necessary to prepare their myristoylated forms. We present purification of myristoylated matrix proteins of the mouse mammary tumor virus and murine leukemia virus, two morphogenetically distinct retroviruses. The proteins were expressed in Escherichia coli coexpressing a yeast N-myristoyltransferase. This E. coli expression system yielded a mixture of myristoylated and nonmyristoylated matrix proteins. We established efficient one-step metal affinity purification that enabled to obtain pure myristoylated matrix proteins suitable for structural and functional studies.
Citace poskytuje Crossref.org
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