Expression and purification of myristoylated matrix protein of Mason-Pfizer monkey virus for NMR and MS measurements.
Protein Expr Purif
; 79(1): 122-7, 2011 Sep.
Article
em En
| MEDLINE
| ID: mdl-21640189
ABSTRACT
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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Base de dados:
MEDLINE
Assunto principal:
Aciltransferases
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Proteínas da Matriz Viral
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Vírus dos Macacos de Mason-Pfizer
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Ácido Mirístico
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Escherichia coli
Idioma:
En
Ano de publicação:
2011
Tipo de documento:
Article