Processed enzymatically active protease (p15 gag ) of avian retrovirus obtained in an E. coli system expressing a recombinant precursor (Pr25 lac‐Δgag )

FEBS Letters

Pečenka, Vladimír¹  Sedláček, Juraj¹  Štrop, Petr²  Kostka, Vladimír²  Kaprálek, František¹  Trávníček, Miloslav¹  Říman, Josef¹ 

[1] Czechoslovak Academy of Sciences, Institute of Molecular Genetics, 166 37 Prague 6, Czechoslovakia;Institute of Organic Chemistry and Biochemistry, 166 37 Prague 6, Czechoslovakia

关键词: Retroviral protease;    Polyprotein precursor processing;    Recombinant product accumulation;    (Myeloblastosis associated virus;    E. coli);   

DOI  :  10.1016/0014-5793(88)80198-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Processing proteases of avian and mammalian retroviruses cut the polyprotein precursors encoded by the retroviral genes into mature functional proteins. Retroviral processing proteases are still a rather poorly characterized group as to their relation to other proteases, specificity, and mechanism of enzymatic action. In avian retroviruses the generation of the processing protease itself comprises a processing cleavage event — the protease p15 ^gag is cut off the carboxy-terminus of a gag polyprotein precursor, Pr76 ^gag . We report here that direct and efficient production of the avian retrovirus processing protease p15 ^gag (required for structure-function studies and rational design of inhibitors) was obtained in an E. coli system, where massive expression of a size-reduced, recombinant precursor (Pr25 ^lac-Δgag was accompanied by its structurally accurate processing.

【 授权许可】

Unknown