Proteolytic activity of the plum pox potyvirus NIa‐protein on excess of natural and artificial substrates in Escherichia coli

FEBS Letters

Riechmann, José Luis¹  Martín, María Teresa¹  Garcia, Juan Antonio¹  Laín, Sonia¹ 

[1] Centro de Biología Molecular (CSIC-UAM), Universidad Autónoma de Madrid, Campus de Cantoblanco, 28049 Madrid, Spain

关键词: Potyvirus;    Viral protease;    Cleavage site;    artificial;    Expression system;    (E. coli);    aa;    amino acids;    nt;    nucleotides;    ORF;    open reading frame;    CP;    capsid protein;    NIa and NIb;    nuclear inclusion protein a and b;    (m)Ab;    (monoclonal) antibody;   

DOI  :  10.1016/0014-5793(89)81550-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The plum pox potyvirus (PPV) NI_a protease expressed from a medium copy number plasmid was able to process an excess of substrate expressed from a high copy number plasmid, in a binary Escherichia coli expression system. The ΔB7 NI_a protease mutant only partially processed the NI_b-CP junction but its efficiency was independent of the amount of substrate. The ΔB7 mutant essentially did not recognize an artificial cleavage site which was quite efficiently recognized by the wild-type protease. No competitive inhibition of the proteolytic activity by the presence of excess of different protease mutants was observed.

【 授权许可】

Unknown