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Eukaryotic initiation factor 4GI is a poor substrate for HIV‐1 proteinase
Author(s) -
Schlick Petra,
Skern Tim
Publication year - 2002
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(02)03415-4
Subject(s) - reticulocyte , proteolysis , cleavage (geology) , protein biosynthesis , viral replication , chemistry , eukaryotic translation , eukaryotic initiation factor , microbiology and biotechnology , biology , biochemistry , translation (biology) , virology , virus , messenger rna , enzyme , gene , paleontology , fracture (geology)
Eukaryotic initiation factor (eIF) 4GI is efficiently cleaved during picornaviral replication. eIF4GI processing has also recently been observed during HIV‐1 replication. We have compared the efficiency of eIF4GI proteolysis in rabbit reticulocyte lysates during translation of mRNAs encoding the foot‐and‐mouth disease virus leader proteinase (L pro ) or the HIV‐1 proteinase (HIV‐1 pro ). L pro cleaved 50% eIF4GI within 12 min whereas HIV‐1 pro required 4 h; the concentrations were 2 pg/μl (0.1 nM) for L pro and 60 pg/μl (2.66 nM) for HIV‐1 pro . HIV‐1 pro processing of eIF4GI is therefore not quantitatively analogous to that of L pro , suggesting that the primary function of eIF4GI cleavage in HIV‐1 replication may not be protein synthesis inhibition.