A novel role for poly(C) binding proteins in programmed ribosomal frameshifting

Sawsan Napthine, Emmely E. Treffers, Susanne Bell, Ian Goodfellow, Ying Fang, Andrew E. Firth, Eric J. Snijder, Ian Brierley

Research output: Contribution to journalArticlepeer-review


Translational control through programmed ribosomal frameshifting (PRF) is exploited widely by viruses and increasingly documented in cellular genes. Frameshifting is induced by mRNA secondary structures that compromise ribosome fidelity during decoding of a heptanucleotide 'slippery' sequence. The nsp2 PRF signal of porcine reproductive and respiratory syndrome virus is distinctive in directing both-2 and-1 PRF and in its requirement for a trans-acting protein factor, the viral replicase subunit nsp1β. Here we show that the the trans-activation of frameshifting is carried out by a protein complex composed of nsp1β and a cellular poly(C) binding protein (PCBP). From the results of in vitro translation and electrophoretic mobility shift assays, we demonstrate that a PCBP/nsp1β complex binds to a C-rich sequence downstream of the slippery sequence and here mimics the activity of a structured mRNA stimulator of PRF. This is the first description of a role for a trans-acting cellular protein in PRF. The discovery broadens the repertoire of activities associated with poly(C) binding proteins and prototypes a new class of virus-host interactions.

Original languageEnglish (US)
Pages (from-to)5491-5503
Number of pages13
JournalNucleic acids research
Issue number12
StatePublished - Jul 8 2016
Externally publishedYes

ASJC Scopus subject areas

  • Genetics


Dive into the research topics of 'A novel role for poly(C) binding proteins in programmed ribosomal frameshifting'. Together they form a unique fingerprint.

Cite this