Expression Profile of Amylolytic Genes in Aspergillus nidulans
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- NAKAMURA Takashi
- Department of Biological Mechanisms and Functions, Graduate School of Bioagricultural Sciences, Nagoya University
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- MAEDA Yuki
- Department of Biological Mechanisms and Functions, Graduate School of Bioagricultural Sciences, Nagoya University
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- TANOUE Nami
- Department of Biological Mechanisms and Functions, Graduate School of Bioagricultural Sciences, Nagoya University
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- MAKITA Tomohiro
- Department of Biological Mechanisms and Functions, Graduate School of Bioagricultural Sciences, Nagoya University
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- KATO Masashi
- Department of Biological Mechanisms and Functions, Graduate School of Bioagricultural Sciences, Nagoya University
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- KOBAYASHI Tetsuo
- Department of Biological Mechanisms and Functions, Graduate School of Bioagricultural Sciences, Nagoya University
Bibliographic Information
- Other Title
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- Expression Profile of Amylolytic Genes in<i>Aspergillus nidulans</i>
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Abstract
Aspergillus nidulans possessed 16 putative amylolytic genes consisting of 7 α-glucosidase (agdA-F), 7 α-amylase (amyA-F), and 2 glucoamylase (glaA and B) genes on the genome. Among them, the agdA, agdB, agdE, agdF, amyA, amyB, amyF, and glaB genes were induced by isomaltose. AmyR, a Zn(II)2Cys6 transcription factor, was required for the induction. The isomaltose-inducible genes possessed at least one consensus sequence for AmyR binding, 5′-CGGN8CGG, on each promoter region. None of the amylolytic genes was induced by maltose.<BR>The mRNA levels of the amylolytic genes except for agdC, amyD, and amyG increased under carbon-starved conditions. Release from CreA-dependent carbon catabolite repression was the main cause of the increase, but, the mRNA levels of agdB, agdF, amyB, amyF, and glaB increased to some extent even in a creA mutant. Therefore, both CreA-dependent and -independent mechanisms are involved in the up-regulation of the amylolytic genes under carbon-starved conditions.
Journal
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 70 (10), 2363-2370, 2006
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Details 詳細情報について
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- CRID
- 1390282681453875840
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- NII Article ID
- 10018525470
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- NII Book ID
- AA10824164
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- COI
- 1:CAS:528:DC%2BD28XhtFynu7%2FN
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- ISSN
- 13476947
- 09168451
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- NDL BIB ID
- 8523689
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- PubMed
- 17031028
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- Abstract License Flag
- Disallowed