ZINC-DEPENDENT STRUCTURE OF A SINGLE-FINGER DOMAIN OF YEAST ADR1
ZINC-DEPENDENT STRUCTURE OF A SINGLE-FINGER DOMAIN OF YEAST ADR1
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DOI：
10.1126/science.3047872
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发表时间：
1988-09-16
期刊：
影响因子：
56.9
通讯作者：
KLEVIT, RE
中科院分区：
文献类型：
--
作者：
PARRAGA, G;HORVATH, SJ;KLEVIT, RE
在提出的“锌指”DNA结合基序中，每个重复单元通过不变的Cys和His残基结合锌金属离子，这驱动每个30个残基单元折叠成独立的核酸结合结构域。为了获得结构信息，我们从酵母转录激活因子ADR1合成了单锌指和双锌指肽，并使用各种光谱技术评估了这些肽的金属结合和DNA结合特性，以及金属稳定结构域的溶液结构。单个锌指可以作为足以进行锌依赖性DNA结合的独立结构存在。实验确定的模型的单指提出，是一致的圆二色性，一维和二维核磁共振，和视觉光谱的单指肽重构锌的存在下。
In the proposed "zinc finger" DNA-binding motif, each repeat unit binds a zinc metal ion through invariant Cys and His residues and this drives the folding of each 30-residue unit into an independent nucleic acid-binding domain. To obtain structural information, we synthesized single and double zinc finger peptides from the yeast transcription activator ADR1, and assessed the metal-binding and DNA-binding properties of these peptides, as well as the solution structure of the metal-stabilized domains, with the use of a variety of spectroscopic techniques. A single zinc finger can exist as an independent structure sufficient for zinc-dependent DNA binding. An experimentally determined model of the single finger is proposed that is consistent with circular dichroism, one- and two-dimensional nuclear magnetic resonance, and visual spectroscopy of the single-finger peptide reconstituted in the presence of zinc.