Mode of AmyR Binding to the CGGN8AGG Sequence in theAspergillus oryzaetaaG2Promoter
| Autor: | Tatsuo Ito, Masashi Kato, Tetsuo Kobayashi, Shuji Tani, Tomoyuki Itoh, Norihiro Tsukagoshi |
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| Rok vydání: | 2004 |
| Předmět: |
Aspergillus oryzae
Applied Microbiology and Biotechnology Biochemistry Analytical Chemistry Fungal Proteins Aspergillus nidulans Electrophoretic mobility shift assay Binding site Promoter Regions Genetic Molecular Biology Gene Binding Sites Base Sequence biology Activator (genetics) Organic Chemistry DNase-I Footprinting Promoter General Medicine biology.organism_classification Molecular biology Gene Expression Regulation Mutagenesis Site-Directed Trans-Activators Protein Binding Biotechnology |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 68:1906-1911 |
| ISSN: | 1347-6947 0916-8451 |
| DOI: | 10.1271/bbb.68.1906 |
| Popis: | AmyR is a transcriptional activator in Aspergillus spp. necessary for induction of the amylolytic enzyme genes. It recognizes 5'-CGGN8CGG-3' conserved in a number of the amylolytic gene promoters, and in addition 5'-CGGAAATTTAA-3' in the A. oryzae alpha-amylase promoter. In this report, interaction of AmyR with the 5'-CGGAAATTTAA-3' type binding site in the Taka-amylase gene (taaG2) promoter was precisely characterized by DNase I footprinting analysis and electrophoretic mobility shift assay in vitro, and also by examination of the in vivo activity of the mutated promoters. The in vitro and in vivo analyses indicated that two AmyR molecules bind cooperatively to the 5'-CGGAAATTTAA-3' sequence by recognizing the CGG triplet at the 5'-end and the AGG triplet just downstream of the sequence. |
| Databáze: | OpenAIRE |
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