期刊
FUNGAL GENETICS AND BIOLOGY
卷 47, 期 3, 页码 254-267出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.fgb.2009.12.004
关键词
Aldolase; Aspergillus nidulans; Carbon metabolism; Gluconeogenesis; Glycolysis
资金
- Greek General Secretariat for Science and Technology [EPETII PENED 03 EDelta/273]
In Aspergillus nidulans the fbaA1013 mutation results in reduced or total loss of growth on glycolytic and gluconeogenic carbon sources, respectively. It also negatively affects growth on several amino acids (including L-proline, L-glutamate or L-aspartate) that the fungus can use as nitrogen source on glycolytic carbon sources. Complementation of the fbaA1013 mutation using an A. nidulans genomic library resulted in cloning of the fbaA gene, which encodes a putative fructose 1,6-biphosphate aldolase (FBA), an enzyme involved in both glycolysis and gluconeogenesis. The fbaA1013 mutation is a chromosome rearrangement in the 51 regulatory region of the fbaA gene resulting in reduced or total loss of transcription in response to glycolytic and gluconeogenic carbon sources respectively. The fbaA gene is essential for growth. A functional FbaA protein is necessary for plasma membrane localization of the AgtA acidic amino acid (L-glutamate/L-aspartate) transporter, as the fbaA1013 mutation results in targeting to and presumably subsequent degradation of AgtA in the vacuole. Our results support a novel role of the FbaA protein that is, involvement in the regulation of amino acids transporters. (C) 2009 Elsevier Inc. All rights reserved.
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