Conformational changes of the N-terminal part of Mason-Pfizer monkey virus p12 protein during multimerization.
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.
Knejzlík
Zdenĕk
Z
Department of Biochemistry and Microbiology, Institute of Chemical Technology, Technická 5, 166 28 Prague 6, Czech Republic.
Ulbrich
Pavel
P
Strohalm
Martin
M
Lastůvková
Hana
H
Kodícek
Milan
M
Sakalian
Michael
M
Ruml
Tomás
T
D002942:Circular Dichroism; D015683:Gene Products, gag / Q000737:chemistry*; D016093:Mason-Pfizer monkey virus / Q000737:chemistry / Q000502:physiology*; D008854:Microscopy, Electron; D011487:Protein Conformation; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D014461:Ultracentrifugation
D015683:Gene Products, gag; C078028:p12 protein, Mason-Pfizer monkey virus