Biomolecular NMR Assignments

, Volume 9, Issue 2, pp 229–233 | Cite as

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

  • Michal DoležalEmail author
  • Richard Hrabal
  • Tomáš Ruml
  • Michaela RumlováEmail author


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.


Isotopic labeling Matrix protein M-PMV Myristoylation Resonance assignment Reverse labeling 



Combined chemical shift perturbation




Isopropyl β-D-1-thiogalactopyranoside


Matrix protein


Mason-Pfizer monkey virus


Phosphatidylinositol 4,5-bisphosphate





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.

Ethical standards

All experiments described comply with the current laws of the Czech Republic.


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Copyright information

© Springer Science+Business Media Dordrecht 2015

Authors and Affiliations

  1. 1.Laboratory of NMR SpectroscopyUniversity of Chemistry and Technology, PraguePragueCzech Republic
  2. 2.Department of Biochemistry and MicrobiologyUniversity of Chemistry and Technology, PraguePragueCzech Republic
  3. 3.Institute of Organic Chemistry and Biochemistry, v.v.i., IOCB and Gilead Research CenterAcademy of Sciences of the Czech RepublicPragueCzech Republic
  4. 4.Department of BiotechnologyUniversity of Chemistry and Technology, PraguePragueCzech Republic

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