Ref ID: 18457
Author:
Tetsuya Hiramoto, Mizuki Tanaka, Ryoko Daidoguchi, Takahiro Shintani, Katsuya Gomi
Author address:
Graduate School of Agricultural Science, Tohoku University
Full conference title:
11 th European Conference on Fungal Genetics
Abstract:
A gene cluster (MAL cluster) involved in maltose utilization is also required for production of amylolytic enzymes in
Aspergillus oryzae. In particular, maltose permease encoded by the gene malP in the MAL cluster is essential for
uptake of maltose that induces the amylolytic genes through the activation of the transcription factor AmyR. The
malP gene expression is induced by maltose and repressed by glucose [1]. However, it has not yet been examined
how MalP is regulated at the protein level in response to carbon sources, although MalP is thought to be degraded
through the endocytic pathway in the presence of glucose as MAL63 in Saccharomyces cerevisiae. In this study, we
examined the effect of various sugar species on endocytosis of the MalP protein.
MalP fused to sGFP (MalP-GFP) localized at the plasma membrane, when expressed by own promoter in maltose
medium. After addition of glucose, MalP-GFP was promptly internalized and delivered to the vacuole. This
internalization was prevented by the addition of latrunculin B, an actin depolymerizing agent, indicating that MalP
was targeted to the vacuole by endocytosis. Effect of the sugar species including glucose analogs on the
internalization of MalP-GFP was investigated by fluorescence microscopy. Consequently, fructose, mannose, and
28208;deoxyglucose as well as glucose triggered the internalization of MalP-GFP to the vacuole, whereas xylose, 68208;
deoxyglucose, and 38208;O8208;methylglucose had no effect on MalP-GFP localization.
[1] Hasegawa et al. Fungal Genet. Biol. 47, 1-9 (2010)
Abstract Number: PR1.38
Conference Year: 2012
Link to conference website: http://www.ecfg.info/images/Abstract_Book_Electronic.pdf
New link: NULL
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