7nbv
Structure of 2A protein from Theilers murine encephalomyelitis virus (TMEV)Structure of 2A protein from Theilers murine encephalomyelitis virus (TMEV)
Structural highlights
Publication Abstract from PubMedThe 2A protein of Theiler's murine encephalomyelitis virus (TMEV) acts as a switch to stimulate programmed -1 ribosomal frameshifting (PRF) during infection. Here, we present the X-ray crystal structure of TMEV 2A and define how it recognises the stimulatory RNA element. We demonstrate a critical role for bases upstream of the originally predicted stem-loop, providing evidence for a pseudoknot-like conformation and suggesting that the recognition of this pseudoknot by beta-shell proteins is a conserved feature in cardioviruses. Through examination of PRF in TMEV-infected cells by ribosome profiling, we identify a series of ribosomal pauses around the site of PRF induced by the 2A-pseudoknot complex. Careful normalisation of ribosomal profiling data with a 2A knockout virus facilitated the identification, through disome analysis, of ribosome stacking at the TMEV frameshifting signal. These experiments provide unparalleled detail of the molecular mechanisms underpinning Theilovirus protein-stimulated frameshifting. Investigating molecular mechanisms of 2A-stimulated ribosomal pausing and frameshifting in Theilovirus.,Hill CH, Cook GM, Napthine S, Kibe A, Brown K, Caliskan N, Firth AE, Graham SC, Brierley I Nucleic Acids Res. 2021 Nov 18;49(20):11938-11958. doi: 10.1093/nar/gkab969. PMID:34751406[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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