Conformational changes of the N-terminal part of Mason-Pfizer monkey virus p12 protein during multimerization

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Abstract

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 α-helix during multimerization. © 2009 Elsevier Inc. All rights reserved.

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Knejzlík, Z., Ulbrich, P., Strohalm, M., Laštůvková, H., Kodíček, M., Sakalian, M., & Ruml, T. (2009). Conformational changes of the N-terminal part of Mason-Pfizer monkey virus p12 protein during multimerization. Virology, 393(1), 168–176. https://doi.org/10.1016/j.virol.2009.07.014

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