Makita Tomohiro, Katsuyama Yoko, Tani Shuji, Suzuki Hayato, Kato Naoki, Todd Richard B, Hynes Michael J, Tsukagoshi Norihiro, Kato Masashi, Kobayashi Tetsuo
Department of Biological Mechanisms and Functions, Graduate School of Bioagricultural Sciences, Nagoya University, Aichi, Japan.
Biosci Biotechnol Biochem. 2009 Feb;73(2):391-9. doi: 10.1271/bbb.80654. Epub 2009 Feb 7.
AmyR is a Zn(II)(2)Cys(6) transcriptional activator that regulates expression of the amylolytic genes in Aspergillus species. Subcellular localization studies of GFP-fused AmyR in A. nidulans 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 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)(2)Cys(6) DNA binding motif.
AmyR是一种Zn(II)(2)Cys(6)转录激活因子，可调节曲霉菌种中淀粉分解基因的表达。对构巢曲霉中绿色荧光蛋白融合的AmyR进行亚细胞定位研究发现，该融合蛋白在淀粉分解基因的生理诱导剂异麦芽糖的作用下优先定位于细胞核。AmyR的C端结构域，命名为MH3（第419 - 496位氨基酸）和MH4（第516 - 542位氨基酸），对于感知诱导刺激和调节亚细胞定位至关重要。位于AmyR中部的MH2结构域（第234 - 375位氨基酸）是靶基因转录激活所必需的，并且在N端Zn(II)(2)Cys(6) DNA结合基序内鉴定出了核定位信号。
