Resonance assignments of the myristoylated Y28F/Y67F mutant of the Mason-Pfizer monkey virus matrix protein

Biomolecular NMR Assignments
Michal DoležalMichaela Rumlová

Abstract

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.

References

Sep 1, 1995·Journal of Biomolecular NMR·D S WishartB D Sykes
Jul 15, 2006·Proceedings of the National Academy of Sciences of the United States of America·Jamil S SaadMichael F Summers
Jan 24, 2007·Journal of Biomolecular NMR·Frank LöhrVolker Dötsch
Jul 24, 2008·Proceedings of the National Academy of Sciences of the United States of America·Jirí VlachTomás Ruml
Sep 24, 2013·Protein Expression and Purification·Michal DoležalMichaela Rumlová
Mar 26, 2014·Protein Expression and Purification·Tomáš KroupaRichard Hrabal

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Citations

Oct 23, 2016·Journal of Molecular Biology·Tomáš KroupaTomáš Ruml

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