大肠杆菌K-12丙氨酸-缬氨酸转氨酶（avtA）基因的克隆与特性分析
Cloning and characterization of the Escherichia coli K-12 alanine-valine transaminase (avtA) gene.
作者信息
Wang M D, Liu L, Wang B M, Berg C M
出版信息
J Bacteriol. 1987 Sep;169(9):4228-34. doi: 10.1128/jb.169.9.4228-4234.1987.
Abstract
avtA, which encodes the alanine-valine transaminase, transaminase C, was cloned in vivo with high- and low-copy-number mini-Mu cloning vectors. The phenotype conferred by the cloned avtA+ gene usually depended upon the plasmid copy number; most high-copy-number avtA+ plasmids permitted isoleucine-requiring ilvE strains to grow in the absence of isoleucine (multicopy suppression), while low-copy-number avtA+ plasmids did not. avtA was mapped to a 1.25-kilobase segment by comparison of the restriction maps of 24 independent mini-Mu plasmids and then by gamma-delta (Tn1000) mutagenesis of a pBR322-avtA+ plasmid. The direction of transcription of avtA on the cloned fragment was determined with fusions to a promoterless lac gene.
摘要
编码丙氨酸 - 缬氨酸转氨酶（转氨酶C）的avtA基因，使用高拷贝数和低拷贝数的微型Mu克隆载体在体内进行克隆。克隆的avtA⁺基因赋予的表型通常取决于质粒拷贝数；大多数高拷贝数的avtA⁺质粒允许需要异亮氨酸的ilvE菌株在没有异亮氨酸的情况下生长（多拷贝抑制），而低拷贝数的avtA⁺质粒则不能。通过比较24个独立的微型Mu质粒的限制性图谱，然后对pBR322 - avtA⁺质粒进行γ-δ（Tn1000）诱变，将avtA定位到一个1.25千碱基的片段上。通过与无启动子的lac基因融合，确定了克隆片段上avtA的转录方向。
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