大肠杆菌色氨酸合成酶α链中第22位和第211位氨基酸残基之间的结构相互作用。
Structural interactions between amino acid residues at positions 22 and 211 in the tryptophan synthetase alpha chain of Escherichia coli.
作者信息
Murgola E J, Yanofsky C
出版信息
J Bacteriol. 1974 Feb;117(2):444-8. doi: 10.1128/jb.117.2.444-448.1974.
Abstract
Construction and characterization of double mutants altered in the structural gene of the tryptophan synthetase alpha chain of Escherichia coli revealed interactions between amino acid residues at positions 22 and 211. These interactions are specific for the particular amino acid residue at position 211. The results indicate also that amino acid residues which appear to be functionally near-equivalent in one configuration may strongly influence the activity of a protein with a subsequent change at another site. Seven independent suppressors of trpA218 (Leu22-Ser211) were isolated. Their properties suggest that all seven may suppress the codon (AGU/C) for Ser211. Six of the seven are co-transducible with glyV, the structural gene for the GGU/C-specific tRNA(Gly).
摘要
对大肠杆菌色氨酸合成酶α链结构基因发生改变的双突变体进行构建和表征，揭示了22位和211位氨基酸残基之间的相互作用。这些相互作用对211位的特定氨基酸残基具有特异性。结果还表明，在一种构型中功能上看似近乎等效的氨基酸残基，可能会在另一个位点发生后续变化时强烈影响蛋白质的活性。分离出了trpA218（Leu22 - Ser211）的七个独立抑制子。它们的特性表明，所有七个抑制子可能都抑制Ser211的密码子（AGU/C）。七个抑制子中有六个与glyV（GGU/C特异性tRNA(Gly)的结构基因）共转导。
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