A novel role for poly(C) binding proteins in programmed ribosomal frameshifting
| Autor: | Sawsan Napthine, Eric J. Snijder, Andrew E. Firth, Susanne Bell, Ian Brierley, Ian Goodfellow, Ying Fang, Emmely E. Treffers |
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| Přispěvatelé: | Napthine, Sawsan [0000-0001-7404-8494], Goodfellow, Ian [0000-0002-9483-510X], Firth, Andrew [0000-0002-7986-9520], Brierley, Ian [0000-0003-3965-4370], Apollo - University of Cambridge Repository |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Swine viruses NAR Breakthrough Article Biology Slippery sequence Ribosome 03 medical and health sciences Eukaryotic translation Genetics Animals Porcine respiratory and reproductive syndrome virus Electrophoretic mobility shift assay RNA Messenger Messenger RNA Translational frameshift Base Sequence 030102 biochemistry & molecular biology Binding protein Frameshifting Ribosomal RNA-Binding Proteins Translation (biology) Molecular biology digestive system diseases 3. Good health Cell biology Cysteine Endopeptidases 030104 developmental biology Multiprotein Complexes Protein Biosynthesis Nucleic Acid Conformation Ribosomes |
| Zdroj: | Nucleic Acids Research Nucleic Acids Research, 44(12), 5491-5503. OXFORD UNIV PRESS |
| ISSN: | 1362-4962 0305-1048 |
| DOI: | 10.1093/nar/gkw480 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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