TARGETING A HERBICIDE-RESISTANT ENZYME FROM ESCHERICHIA-COLI TO CHLOROPLASTS OF HIGHER-PLANTS
TARGETING A HERBICIDE-RESISTANT ENZYME FROM ESCHERICHIA-COLI TO CHLOROPLASTS OF HIGHER-PLANTS
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DOI：
10.1038/nbt0687-579
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发表时间：
1987-06-01
期刊：
影响因子：
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通讯作者：
KISHORE, GM
中科院分区：
文献类型：
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作者：
DELLACIOPPA, G;BAUER, SC;KISHORE, GM
5 -烯醇式莽草酸-3-磷酸（EPSP）合成酶是植物中莽草酸途径的叶绿体定位酶。该酶合成为具有N-末端转运肽序列的细胞质前体，所述N-末端转运肽序列在转录后指导输入叶绿体。EPSP合酶具有重要的农艺学意义，因为它是除草剂中的活性成分草甘膦的主要靶标。Roundup®.将编码EPSP合酶突变体、草甘膦抗性形式的大肠杆菌基因融合在编码矮牵牛EPSP合酶转运肽序列的cDNA的一部分之后。通过基因融合体的体外转录和翻译产生的嵌合酶被迅速导入叶绿体，并进行蛋白水解处理，得到稳定的草甘膦抗性酶。
5 – Enolpyruvylshikimate – 3 – phosphate (EPSP) synthase is a chloroplast–localized enzyme of the shikimate pathway in plants. The enzyme is synthesized as a cytoplasmic precursor with an N–terminal transit peptide sequence that post–translationally directs import into chloroplasts. EPSP synthase is of significant agronomic importance because it is the primary target for glyphosate, the active ingredient in the herbicide. Roundup®. A gene fromEscherichia coliencoding a mutant, glyphosate resistant form of EPSP synthase was fused behind a portion of the cDNA that encodes the transit peptide sequence ofPetunia hybridaEPSP synthase. A chimeric enzyme, produced byin vitrotranscription and translation of the gene fusion, was rapidly imported into chloroplasts and proteolytically processed to give a stable, glyphosate resistant enzyme.