SEQUENCE REQUIREMENTS FOR COILED-COILS - ANALYSIS WITH LAMBDA-REPRESSOR-GCN4 LEUCINE ZIPPER FUSIONS
SEQUENCE REQUIREMENTS FOR COILED-COILS - ANALYSIS WITH LAMBDA-REPRESSOR-GCN4 LEUCINE ZIPPER FUSIONS
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DOI：
10.1126/science.2147779
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发表时间：
1990-12-07
期刊：
影响因子：
56.9
通讯作者：
SAUER, RT
中科院分区：
文献类型：
--
作者：
HU, JC;OSHEA, EK;SAUER, RT
在大肠杆菌中建立了以噬菌体λ抑制子的氨基末端结构域为二聚化报告的研究亮氨酸拉链的遗传系统。该系统被用来分析酵母转录激活剂GCN4中形成亮氨酸拉链二聚体疏水界面的8个位置的氨基酸侧链的重要性。当分析单个氨基酸替换时，大多数功能变异体在二聚体界面上含有疏水残基，而大多数非功能序列变异体含有强极性或螺旋断裂残基。然而，在多个随机实验中，许多疏水残基的组合被发现是无功能的，并且七肽重复中的亮氨酸在亮氨酸拉链二聚中具有特殊的功能。
A genetic system was developed inEscherichia colito study leucine zippers with the amino-terminal domain of bacteriophage λ repressor as a reporter for dimerization. This system was used to analyze the importance of the amino acid side chains at eight positions that form the hydrophobic interface of the leucine zipper dimer from the yeast transcriptional activator, GCN4. When single amino acid substitutions were analyzed, most functional variants contained hydrophobic residues at the dimer interface, while most nonfunctional sequence variants contained strongly polar or helix-breaking residues. In multiple randomization experiments, however, many combinations of hydrophobic residues were found to be nonfunctional, and leucines in the heptad repeat were shown to have a special function in leucine zipper dimerization.