Conformational changes of the N-terminal part of Mason-Pfizer monkey virus p12 protein during multimerization
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, Research Support, N.I.H., Extramural, práce podpořená grantem
Grantová podpora
CA 27834
NCI NIH HHS - United States
PubMed
19699504
DOI
10.1016/j.virol.2009.07.014
PII: S0042-6822(09)00449-8
Knihovny.cz E-zdroje
- MeSH
- cirkulární dichroismus MeSH
- elektronová mikroskopie MeSH
- genové produkty gag chemie MeSH
- konformace proteinů MeSH
- kvarterní struktura proteinů MeSH
- Masonův-Pfizerův opičí virus chemie fyziologie MeSH
- multimerizace proteinu * MeSH
- terciární struktura proteinů MeSH
- ultracentrifugace MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Research Support, N.I.H., Extramural MeSH
- Názvy látek
- genové produkty gag MeSH
- p12 protein, Mason-Pfizer monkey virus MeSH Prohlížeč
The Mason-Pfizer monkey virus is a prototype Betaretrovirus with the defining characteristic that it assembles spherical immature particles from Gag-related polyprotein precursors within the cytoplasm of the infected cell. It was shown previously that the N-terminal part of the Gag p12 domain (wt-Np12) is required for efficient assembly. However, the precise role for p12 in mediating Gag-Gag interaction is still poorly understood. In this study we employed detailed circular dichroism spectroscopy, electron microscopy and ultracentrifugation analyses of recombinant wt-Np12 prepared by in vitro transcription and translation. The wt-Np12 domain fragment forms fibrillar structures in a concentration-dependent manner. Assembly into fibers is linked to a conformational transition from unfolded or another non-periodical state to alpha-helix during multimerization.
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