Resonance assignments of the myristoylated Y28F/Y67F mutant of the Mason-Pfizer monkey virus matrix protein
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The matrix protein (MA) of the Mason-Pfizer monkey virus (M-PMV) plays a key role in the transport and budding of immature retroviral particles from the host cell. Natural N-terminal myristoylation of MA is essential for the targeting of the particles to the plasma membrane and participates in the interaction of MA with membranes phospholipids. The mutation Y28F/Y67F in MA reduces budding and thus causes the accumulation of viral particles under the cytoplasmic membrane. To investigate the impact of Y28F/Y67F mutation on the structure of MA, we prepared this protein in amount and quality suitable for NMR spectroscopy. We report backbone, side-chain and myristoyl residue assignments of the Y28F/Y67F mutant of the M-PMV matrix protein, which will be used to study the interaction with membrane phospholipids and to determine the structure of the mutant matrix protein.
KeywordsIsotopic labeling Matrix protein M-PMV Myristoylation Resonance assignment Reverse labeling
Combined chemical shift perturbation
Mason-Pfizer monkey virus
This work was supported by Czech Science Foundation Grant P302/12/1895.
Conflict of interest
The authors declare that they have no conflict of interest.
All experiments described comply with the current laws of the Czech Republic.
- Wishart DS, Bigam CG, Yao J et al (1995) 1H, 13C and 15N chemical shift referencing in biomolecular NMR. J Biomol NMR 6:135–140Google Scholar
- Yamazaki T, Forman-Kay JD, Kay LE (1993) Two-dimensional NMR experiments for correlating 13Cβ and 1Hδ/ε chemical shifts of aromatic residues in 13C-labeled proteins via scalar couplings. J Am Chem Soc 115:11054–11055. doi: 10.1021/ja00076a099