Subcellular localization of aphidicolin biosynthetic enzymes heterologously expressed in Aspergillus oryzae

Akihiko Ban, Mizuki Tanaka, Ryuya Fujii, Atsushi Minami, Hideaki Oikawa, Takahiro Shintani, Katsuya Gomi

研究成果: Article査読

3 被引用数 (Scopus)

抄録

The secondary metabolite aphidicolin has previously been produced by Aspergillus oryzae after the heterologous expression of four biosynthetic enzymes isolated from Phoma betae. In this study, we examined the subcellular localization of aphidicolin biosynthetic enzymes in A. oryzae. Fusion of green fluorescent protein to each enzyme showed that geranylgeranyl diphosphate synthase and terpene cyclase are localized to the cytoplasm and the two monooxygenases (PbP450-1 and PbP450-2) are localized to the endoplasmic reticulum (ER). Protease protection assays revealed that the catalytic domain of both PbP450s was cytoplasmic. Deletion of transmembrane domains from both PbP450s resulted in the loss of ER localization. Particularly, a PbP450-1 mutant lacking the transmembrane domain was localized to dot-like structures, but did not colocalize with any known organelle markers. Aphidicolin biosynthesis was nearly abrogated by deletion of the transmembrane domain from PbP450-1. These results suggest that ER localization of PbP450-1 is important for aphidicolin biosynthesis.

本文言語English
ページ(範囲)139-147
ページ数9
ジャーナルBioscience, Biotechnology and Biochemistry
82
1
DOI
出版ステータスPublished - 2018

ASJC Scopus subject areas

  • バイオテクノロジー
  • 分析化学
  • 生化学
  • 応用微生物学とバイオテクノロジー
  • 分子生物学
  • 有機化学

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