PROTEOLYTIC ACTIVITY OF THE PLUM POX POTYVIRUS NIA-PROTEIN ON EXCESS OF NATURAL AND ARTIFICIAL SUBSTRATES IN ESCHERICHIA-COLI
PROTEOLYTIC ACTIVITY OF THE PLUM POX POTYVIRUS NIA-PROTEIN ON EXCESS OF NATURAL AND ARTIFICIAL SUBSTRATES IN ESCHERICHIA-COLI
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DOI：
10.1016/0014-5793(89)81550-9
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发表时间：
1989-11-06
期刊：
影响因子：
3.5
通讯作者：
LAIN, S
中科院分区：
文献类型：
--
作者：
GARCIA, JA;RIECHMANN, JL;LAIN, S
在大肠杆菌双表达系统中，由中等拷贝数质粒表达的李痘马铃薯Y病毒（PPV）NI α蛋白酶能够处理由高拷贝数质粒表达的过量底物。ΔB7 NIa蛋白酶突变体仅部分加工NIb-CP连接，但其效率与底物量无关。ΔB7突变体基本上不识别被野生型蛋白酶相当有效地识别的人工切割位点。没有观察到过量的不同蛋白酶突变体的存在对蛋白水解活性的竞争性抑制。
The plum pox potyvirus (PPV) NIaprotease expressed from a medium copy number plasmid was able to process an excess of substrate expressed from a high copy number plasmid, in a binaryEscherichia coliexpression system. The ΔB7 NIaprotease mutant only partially processed the NIb‐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.