FEBS Letters | |
Cleavage of translation initiation factor 4AI (eIF4AI) but not eIF4AII by foot‐and‐mouth disease virus 3C protease: identification of the eIF4AI cleavage site | |
Belsham, Graham J.1  Ross-Smith, Natalie1  Li, Wei2  Proud, Christopher G.2  | |
[1] BBSRC Institute for Animal Health, Pirbright, Woking, Surrey GU24 ONF, UK;School of Life Sciences, MSI/WTB Complex, University of Dundee, Dundee DD1 5EH, UK | |
关键词: Picornavirus; Translation initiation factor eIF4A; Protein synthesis; 3C protease; Foot-and-mouth disease virus; FMDV; foot-and-mouth disease virus; IRES; internal ribosome entry site; PV; poliovirus; EMCV; encephalomyocarditis virus; IPTG; isopropyl β-D-thiogalactoside; PCR; polymerase chain reaction; | |
DOI : 10.1016/S0014-5793(01)02885-X | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
The translation initiation factor eIF4A is cleaved within mammalian cells infected by foot-and-mouth disease virus (FMDV). The FMDV 3C protease cleaves eIF4AI (between residues E143 and V144), but not the closely related eIF4AII. Modification of eIF4AI, to produce a sequence identical to eIF4AII around the cleavage site, blocked proteolysis. Alignment of mammalian eIF4AI onto the three-dimensional structure of yeast eIF4A located the scissile bond within an exposed, flexible portion of the molecule. The N- and C-terminal cleavage products of eIF4AI generated by FMDV 3C dissociate. Cleavage of eIF4AI by FMDV 3C is thus expected to inactivate it.
【 授权许可】
Unknown
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