大肠杆菌lacZ基因内形成活性杂合β-半乳糖苷酶分子的位点。
Sites within gene lacZ of Escherichia coli for formation of active hybrid beta-galactosidase molecules.
作者信息
Brickman E, Silhavy T J, Bassford P J, Shuman H A, Beckwith J R
出版信息
J Bacteriol. 1979 Jul;139(1):13-8. doi: 10.1128/jb.139.1.13-18.1979.
Abstract
We describe the genetic analysis of 21 Escherichia coli strains in which the amino-terminal sequence of beta-galactosidase has been removed and replaced by an amino-terminal sequence from one or another of the proteins involved in maltose transport. Genetic mapping of the lacZ end of these fused genes indicates that only those fusions in which fewer than 41 amino acids are removed from the amino-terminal sequence of beta-galactosidase result in enzymatically active molecules. Within the region between amino acid 17 and amino acid 41 there are at least four or five sites where enzymatically active hybrid proteins can be formed.
摘要
我们描述了对21株大肠杆菌的遗传分析，这些菌株中β-半乳糖苷酶的氨基末端序列已被去除，并被参与麦芽糖转运的一种或另一种蛋白质的氨基末端序列所取代。这些融合基因的lacZ末端的遗传图谱表明，只有那些从β-半乳糖苷酶的氨基末端序列中去除少于41个氨基酸的融合才会产生具有酶活性的分子。在氨基酸17至氨基酸41之间的区域内，至少有四到五个位点可以形成具有酶活性的杂合蛋白。
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Isolation of the bacteriophage lambda receptor from Escherichia coli.从大肠杆菌中分离噬菌体λ受体
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