Expression and purification of myristoylated matrix protein of Mason-Pfizer monkey virus for NMR and MS measurements.
 

Expression and purification of myristoylated matrix protein of Mason-Pfizer monkey virus for NMR and MS measurements.

Expression and purification of myristoylated matrix protein of Mason-Pfizer monkey virus for NMR and MS measurements.

Protein Expr Purif. 2011 May 24;

Authors: Prchal J, Junkova P, Strmiskova M, Lipov J, Hynek R, Ruml T, Hrabal R

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.

PMID: 21640189 [PubMed - as supplied by publisher]



Source: PubMed