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Expression and purification of myristoylated matrix protein of Mason-Pfizer monkey virus for NMR and MS measurements
J. Prchal, P. Junkova, M. Strmiskova, J. Lipov, R. Hynek, T. Ruml, R. Hrabal,
Language English Country United States
Document type Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't
- MeSH
- Acyltransferases chemistry genetics isolation & purification MeSH
- Escherichia coli enzymology genetics MeSH
- Gene Expression MeSH
- Myristic Acid chemistry MeSH
- Mason-Pfizer monkey virus chemistry genetics MeSH
- Nuclear Magnetic Resonance, Biomolecular MeSH
- Viral Matrix Proteins chemistry genetics isolation & purification MeSH
- Recombinant Fusion Proteins chemistry genetics isolation & purification MeSH
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Research Support, N.I.H., Extramural MeSH
Matrix proteins play multiple roles both in early and late stages of the viral replication cycle. Their N-terminal myristoylation is important for interaction with the host cell membrane during virus budding. We used Escherichia coli, carrying N-myristoyltransferase gene, for the expression of the myristoylated His-tagged matrix protein of Mason-Pfizer monkey virus. An efficient, single-step purification procedure eliminating all contaminating proteins including, importantly, the non-myristoylated matrix protein was designed. The comparison of NMR spectra of matrix protein with its myristoylated form revealed substantial structural changes induced by this fatty acid modification.
References provided by Crossref.org
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- $a Matrix proteins play multiple roles both in early and late stages of the viral replication cycle. Their N-terminal myristoylation is important for interaction with the host cell membrane during virus budding. We used Escherichia coli, carrying N-myristoyltransferase gene, for the expression of the myristoylated His-tagged matrix protein of Mason-Pfizer monkey virus. An efficient, single-step purification procedure eliminating all contaminating proteins including, importantly, the non-myristoylated matrix protein was designed. The comparison of NMR spectra of matrix protein with its myristoylated form revealed substantial structural changes induced by this fatty acid modification.
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