Extremely efficient cleavage of eIF4G by picornaviral proteinases L and 2A in vitro

FEBS Letters

Skern, Tim¹  Glaser, Walter¹ 

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

关键词: Foot-and-mouth disease L proteinase;    Human rhinovirus 2A proteinase;    Picornavirus;    eIF4G cleavage;    Inhibition of protein synthesis;    Initiation of translation;   

DOI  :  10.1016/S0014-5793(00)01928-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown