Nonmyristoylated matrix protein from the Mason-Pfizer monkey virus forms oligomers
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't
Grant support
CA 27834
NCI NIH HHS - United States
PubMed
19481092
DOI
10.1016/j.jmb.2009.05.063
PII: S0022-2836(09)00645-7
Knihovny.cz E-resources
- MeSH
- Diffusion MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Kinetics MeSH
- Protein Structure, Quaternary * MeSH
- Myristic Acid metabolism MeSH
- Magnetic Resonance Spectroscopy MeSH
- Mason-Pfizer monkey virus chemistry MeSH
- Models, Molecular MeSH
- Molecular Sequence Data MeSH
- Protein Multimerization drug effects MeSH
- Mutant Proteins chemistry MeSH
- Oxidation-Reduction drug effects MeSH
- Viral Matrix Proteins chemistry MeSH
- Cross-Linking Reagents pharmacology MeSH
- Amino Acid Sequence MeSH
- Sequence Alignment MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Research Support, N.I.H., Extramural MeSH
- Names of Substances
- Myristic Acid MeSH
- Mutant Proteins MeSH
- Viral Matrix Proteins MeSH
- Cross-Linking Reagents MeSH
We studied the oligomeric properties of betaretroviral nonmyristoylated matrix protein (MA) and its R55F mutant from the Mason-Pfizer monkey virus in solution by means of chemical crosslinking and NMR spectroscopy. By analyzing crosslinked products and using concentration-dependent NMR chemical shift mapping, we have proven that the wild-type (WT) MA forms oligomers in solution. Conversely, no oligomerization was observed for the R55F mutant. Structural comparison of MAs explained their different behaviors in solution, concluding that the key residues involved in intermonomeric interaction are exposed in the WT MA but buried in the mutant, preventing the oligomerization of R55F. The final model of oligomerization of the WT MA was derived by concerted use of chemical shift mapping and diffusion-ordered spectroscopy measured on a set of protein samples with varying concentrations. We found that the Mason-Pfizer monkey virus WT MA exists in a monomer-dimer-trimer equilibrium in solution, with the corresponding dissociation constants of 2.3 and 0.24 mM, respectively. Structures of the oligomers calculated with HADDOCK software are closely related to the structures of other retroviral MA trimers.
References provided by Crossref.org
Interaction Interface of Mason-Pfizer Monkey Virus Matrix and Envelope Proteins
Myristoylation drives dimerization of matrix protein from mouse mammary tumor virus
