| Literature DB >> 19202286 |
Tomohiro Makita1, Yoko Katsuyama, Shuji Tani, Hayato Suzuki, Naoki Kato, Richard B Todd, Michael J Hynes, Norihiro Tsukagoshi, Masashi Kato, Tetsuo Kobayashi.
Abstract
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.Entities:
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Year: 2009 PMID: 19202286 DOI: 10.1271/bbb.80654
Source DB: PubMed Journal: Biosci Biotechnol Biochem ISSN: 0916-8451 Impact factor: 2.043