- 【Updated on May 12, 2025】 Integration of CiNii Dissertations and CiNii Books into CiNii Research
- Trial version of CiNii Research Knowledge Graph Search feature is available on CiNii Labs
- 【Updated on June 30, 2025】Suspension and deletion of data provided by Nikkei BP
- Regarding the recording of “Research Data” and “Evidence Data”
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
Bibliographic Information
- Other Title
-
- 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
Search this article
Description
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.
Journal
-
- Food Preservation Science
-
Food Preservation Science 33 (1), 9-13, 2007
Japan Association of Food Preservation Scientists
- Tweet
Details 詳細情報について
-
- CRID
- 1390282680093660672
-
- NII Article ID
- 10018852497
-
- NII Book ID
- AA11178236
-
- COI
- 1:CAS:528:DC%2BD2sXktVCit7w%3D
-
- ISSN
- 21861277
- 13441213
-
- NDL BIB ID
- 8736057
-
- Text Lang
- en
-
- Article Type
- journal article
-
- Data Source
-
- JaLC
- IRDB
- NDL Search
- Crossref
- CiNii Articles
- OpenAIRE
-
- Abstract License Flag
- Disallowed