Isolation and Transcriptional Regulation of the Fructose 1,6-Bisphosphate Aldolase Gene FBA1 in the Psychrophilic Yeast Cystofilobasidium capitatum

  • FUJIMURA Shuki
    Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture
  • UCHINO Masataka
    Department of Applied Biology and Chemistry, Faculty of Applied Bioscience, Tokyo University of Agriculture
  • ITO Takashi
    Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture
  • MYODA Takao
    Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture
  • NAGAOKA Toshinori
    Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture
  • MIYAJI Tatsuro
    Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture
  • NAKAGAWA Tomoyuki
    Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture
  • TAKANO Katsumi
    Department of Applied Biology and Chemistry, Faculty of Applied Bioscience, Tokyo University of Agriculture
  • TOMIZUKA Noboru
    Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture

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  • 低温性酵母 <I>Cystofilobasidium capitatum</I>由来アルドラーゼの一次構造とその発現制御

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Abstract

In this study, we report the primary structure of fructose 1, 6-bisphosphate aldolase encoded by Cystofilobasidium capitatum FBAl (CcFBAl) and the regulation of its gene expression. CcFBAl consists of a 1, 080 bp ORF corresponding to a protein of 360 amino acid residues, and the calculated molecular weight of CcFbalp is 39, 626 Da. The CcFbalp has both aldolase class-II signatures 1 and 2. CcFBAl is expressed at the same level during growth on several different carbon sources, although expression level may be slightly higher on glucose. Transcription of CcFBAl is not influenced by temperature or existence of oxygen, although it was reduced during the stationary phase. We show that CcFbalp is a constitutive enzyme in C. capitatum, and suggest that FBAl could be used as a marker for the detection of pectinolytic psychrophilic yeasts using the PCR method.

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