Eukaryotic initiation factor 4GI is a poor substrate for HIV‐1 proteinase

FEBS Letters

Skern, Tim¹  Schlick, Petra¹ 

[1] Institute for Medical Biochemistry, Division of Biochemistry, University of Vienna, Dr. Bohr-Gasse 9/3, A-1030 Vienna, Austria

关键词: Retrovirus;    Human immunodeficiency disease virus;    Picornavirus;    Foot-and-mouth disease virus;    eIF4G cleavage;    Initiation of translation;    eIF4G;    eukaryotic initiation factor 4G;    FMDV;    foot-and-mouth disease virus;    Lpro;    leader proteinase;    PAGE;    polyacrylamide gel electrophoresis;    RRL;    rabbit reticulocyte lysate;   

DOI  :  10.1016/S0014-5793(02)03415-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown