通过异核核磁共振光谱检测发现，酵母热休克转录因子的N端激活结构域呈无结构状态。
Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy.
作者信息
Cho H S, Liu C W, Damberger F F, Pelton J G, Nelson H C, Wemmer D E
机构信息
Department of Chemistry, University of California, Berkeley 94720, USA.
出版信息
Protein Sci. 1996 Feb;5(2):262-9. doi: 10.1002/pro.5560050210.
Abstract
The structure and dynamics of the N-terminal activation domains of the yeast heat shock transcription factors of Kluyveromyces lactis and Saccharomyces cerevisiae were probed by heteronuclear 15N[1H] correlation and 15N[1H] NOE NMR studies. Using the DNA-binding domain as a structural reference, we show that the protein backbone of the N-terminal activation domain undergoes rapid, large-amplitude motions and is therefore unstructured. Difference CD data also show that the N-terminal activation domain remains random-coil, even in the presence of DNA. Implications for a "polypeptide lasso" model of transcriptional activation are discussed.
摘要
通过异核15N[1H]相关和15N[1H] NOE核磁共振研究，对乳酸克鲁维酵母和酿酒酵母的酵母热休克转录因子N端激活结构域的结构和动力学进行了探究。以DNA结合结构域作为结构参考，我们发现N端激活结构域的蛋白质主链经历快速、大幅度的运动，因此是无结构的。差异圆二色性数据也表明，即使存在DNA，N端激活结构域仍保持无规卷曲。文中讨论了转录激活的“多肽套索”模型的相关意义。
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