大肠杆菌thrA基因的核苷酸序列。
Nucleotide sequence of the thrA gene of Escherichia coli.
作者信息
Katinka M, Cossart P, Sibilli L, Saint-Girons I, Chalvignac M A, Le Bras G, Cohen G N, Yaniv M
出版信息
Proc Natl Acad Sci U S A. 1980 Oct;77(10):5730-3. doi: 10.1073/pnas.77.10.5730.
Abstract
The thrA gene of Escherichia coli codes for a single polypeptide chain having two enzymatic activities required for the biosynthesis of threonine, aspartokinase I and homoserine dehydrogenase I. This gene was cloned in a bacterial plasmid and its complete nucleotide sequence was established. It contains 2460 base pairs that encode for a polypeptide chain of 820 amino acids. The previously determined partial amino acid sequence of this protein is in good agreement with that predicted from the nucleotide sequence. The gene contains an internal sequence that resembles the structure of bacterial ribosome-binding sites, with an AUG preceded by four triplets, each of which can be converted to a nonsense codon by a single mutation. This suggests that the single polypeptide chain was formed by the fusion of two genes and that initiation of translation may occur inside the gene to give a protein fragment having only the homoserine dehydrogenase activity.
摘要
大肠杆菌的thrA基因编码一条单一的多肽链，该多肽链具有苏氨酸生物合成所需的两种酶活性，即天冬氨酸激酶I和高丝氨酸脱氢酶I。此基因被克隆到一个细菌质粒中，并确定了其完整的核苷酸序列。它包含2460个碱基对，编码一条由820个氨基酸组成的多肽链。先前测定的该蛋白质的部分氨基酸序列与从核苷酸序列预测的结果高度一致。该基因包含一个内部序列，类似于细菌核糖体结合位点的结构，在一个AUG之前有四个三联体，每个三联体通过单个突变都可转变为无义密码子。这表明这条单一的多肽链是由两个基因融合形成的，并且翻译起始可能发生在基因内部，从而产生仅具有高丝氨酸脱氢酶活性的蛋白质片段。
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