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Cleavage of translation initiation factor 4AI (eIF4AI) but not eIF4AII by foot‐and‐mouth disease virus 3C protease: identification of the eIF4AI cleavage site
Author(s) -
Li Wei,
Ross-Smith Natalie,
Proud Christopher G.,
Belsham Graham J.
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02885-x
Subject(s) - cleavage (geology) , scissile bond , foot and mouth disease virus , proteolysis , protease , picornavirus , eukaryotic translation , biology , virology , virus , cleavage factor , aphthovirus , chemistry , internal ribosome entry site , translation (biology) , biochemistry , rna , enzyme , ribosome , messenger rna , gene , fracture (geology) , paleontology
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.