Cotranslational folding stimulates programmed ribosomal frameshifting in the alphavirus structural polyprotein.

ABSTRACT: Viruses maximize their genetic coding capacity through a variety of biochemical mechanisms, including programmed ribosomal frameshifting (PRF), which facilitates the production of multiple proteins from a single mRNA transcript. PRF is typically stimulated by structural elements within the mRNA that generate mechanical tension between the transcript and ribosome. However, in this work, we show that the forces generated by the cotranslational folding of the nascent polypeptide chain can also enhance PRF. Using an array of biochemical, cellular, and computational techniques, we first demonstrate that the Sindbis virus structural polyprotein forms two competing topological isomers during its biosynthesis at the ribosome-translocon complex. We then show that the formation of one of these topol

SUBMITTER: Harrington HR 

PROVIDER: S-EPMC7242702 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature