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Extremely efficient cleavage of eIF4G by picornaviral proteinases L and 2A in vitro
Author(s) -
Glaser Walter,
Skern Tim
Publication year - 2000
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(00)01928-1
Subject(s) - cleavage (geology) , in vitro , eif4g , chemistry , biochemistry , biophysics , microbiology and biotechnology , biology , messenger rna , paleontology , translation (biology) , fracture (geology) , gene
Certain picornaviruses encode proteinases which cleave the translation initiation factor eIF4G, a member of the eIF4F complex which recruits mRNA to the 40S ribosomal subunit during initiation of protein synthesis in eukaryotes. We have compared the efficiency of eIF4G cleavage in rabbit reticulocyte lysates during translation of mRNAs encoding the foot‐and‐mouth disease virus leader proteinase (L pro ) or the human rhinovirus 2A pro . Under standard translation conditions, L pro cleaved 50% of eIF4G within 4 min after initiation of protein synthesis, whereas 2A pro required 15 min. At these times, the molar ratios of proteinase to eIF4G were 1:130 for L pro and 1:12 for 2A pro , indicating a much more efficient in vitro cleavage than previously observed. The molar ratios are similar to those observed during viral infection in vivo.