Co-folding and RNA activation of poliovirus 3C^pro polyprotein precursors.

ABSTRACT: Positive-strand RNA viruses use long open reading frames to express large polyproteins that are processed into individual proteins by viral proteases. Polyprotein processing is highly regulated and yields intermediate species with different functions than the fully processed proteins, increasing the biochemical diversity of the compact viral genome while also presenting challenges in that proteins must remain stably folded in multiple contexts. We have used circular dichroism spectroscopy and single molecule microscopy to examine the solution structure and self-association of the poliovirus P3 region protein composed of membrane binding 3A, RNA priming 3B (VPg), 3C^pro protease, and 3D^pol RNA-dependent RNA polymerase proteins. Our data indicate that co-folding interact

SUBMITTER: Campagnola G 

PROVIDER: S-EPMC10590986 | biostudies-literature | 2023 Nov

REPOSITORIES: biostudies-literature