Synergy of importin α recognition and DNA binding by the yeast transcriptional activator GAL4
Synergy of importin α recognition and DNA binding by the yeast transcriptional activator GAL4
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DOI：
10.1016/s0014-5793(99)01515-x
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发表时间：
1999-11-26
期刊：
影响因子：
3.5
通讯作者：
Jans, DA
中科院分区：
文献类型：
--
作者：
Chan, CK;Jans, DA
酵母转录激活子GAL4的n端包含部分重叠的核靶向和DNA结合功能。我们之前已经证明，GAL4被输入蛋白β以高亲和力识别，而不是被传统的核定位序列结合输入蛋白α / β异源二聚体的输入蛋白α亚基识别。本研究使用基于elisa的结合和电泳迁移量转移试验表明，输入蛋白α可以识别GAL4，但只有当GAL4与特定的DNA识别序列结合时才会发生。有趣的是，通过输入α增强GAL4部分的DNA结合，这意味着这两种功能之间的协同合作。研究结果表明，除了α蛋白在核运输中的既定作用外，α蛋白在细胞核中的输入可能也有作用，同时GAL4作为DNA载体在基因治疗中的应用也有意义。(C) 1999年欧洲生化学会联合会。
The N-terminus of the yeast transcriptional activator GAL4 contains partially overlapping nuclear targeting and DNA binding functions. We have previously shown that GAL4 is recognised with high affinity by importin beta and not by the conventional nuclear localisation sequence binding importin alpha subunit of the importin alpha/beta heterodimer, The present study uses ELISA-based binding and electrophoretic mobility shift assays to show that recognition of GAL4 by importin alpha can occur, but only when GAL4 is bound to its specific DNA recognition sequence. Intriguingly, binding by importin alpha enhances DNA binding on the part of GAL4, implying a synergistic co-operation between these two functions. The results implicate a possible role for importin alpha in the nucleus additional to its established role in nuclear transport, as well as having implications for the use of GAL4 as a DNA carrier in gene therapy applications. (C) 1999 Federation of European Biochemical Societies.