Cleavage of translation initiation factor 4AI (eIF4AI) but not eIF4AII by foot-and-mouth disease virus 3C protease: identification of the eIF4AI cleavage site

Wei Li, Natalie Ross-Smith, Christopher G. Proud, Graham Belsham

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

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. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
Original languageEnglish
JournalF E B S Letters
Volume507
Issue number1
Pages (from-to)1-5
ISSN0014-5793
DOIs
Publication statusPublished - 2001
Externally publishedYes

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