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.
Copyright © 2011 Elsevier Inc. All rights reserved.
Publication types
-
Research Support, N.I.H., Extramural
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Acyltransferases / chemistry
-
Acyltransferases / genetics*
-
Acyltransferases / isolation & purification
-
Escherichia coli / enzymology*
-
Escherichia coli / genetics*
-
Gene Expression
-
Mason-Pfizer monkey virus / chemistry
-
Mason-Pfizer monkey virus / genetics*
-
Myristic Acid / chemistry*
-
Nuclear Magnetic Resonance, Biomolecular
-
Recombinant Fusion Proteins / chemistry
-
Recombinant Fusion Proteins / genetics
-
Recombinant Fusion Proteins / isolation & purification
-
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
-
Viral Matrix Proteins / chemistry*
-
Viral Matrix Proteins / genetics*
-
Viral Matrix Proteins / isolation & purification
Substances
-
Recombinant Fusion Proteins
-
Viral Matrix Proteins
-
Myristic Acid
-
Acyltransferases
-
glycylpeptide N-tetradecanoyltransferase