Inducer dependent nudear entry of a fungal transctiptian factorAmyR

AmyR是一种锌(II)_2Cys_6转录激活剂，在曲霉属中调节淀粉酶基因的表达。GFP融合AmyR的亚细胞定位研究表明，融合蛋白优先定位于细胞核，而异麦芽糖是淀粉分解基因的生理诱导剂。AmyR的C-末端结构域，分别命名为MH3(残基419-496)和MH4(残基516-542)，是感受诱导刺激和调节亚细胞定位所必需的。位于AmyR中间的MH2结构域(残基234-375)是转录激活靶基因所必需的，核定位信号存在于N-末端的锌(II)_2Cys_6DNA结合基序中。对MH3结构域的突变分析表明，复杂的Lite结构域相互作用调节AmyR的核定位和活性

AmyR is a Zn (II)_2Cys_6 transcriptional activator that regulates expression of the amylolytic genes in Aspergillus species. Subcellular localization studies of GFP fused AmyR revealed that the fusion protein preferentially localized to the nucleus in response to isomaltose, the physiological inducer of the amylolytic genes. The C-terminal domains of AmyR, designated as MH3 (residues 419-496) and MH4 (residues 516-542), were essential for sensing the inducing stimulus and regulating the subcellular localization. The MH2 domain (residues 234-375) located in the middle of AmyR was required for transcriptional activation of the target genes, and the nuclear localization signals were identified within the N-terminal Zn (II) _2Cys_6 DNA binding motif. Mutational analysis of the MH3 domain suggested that complex liter domain interactions regulate nuclear localization and activity of AmyR