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ID 59909
フルテキストURL
著者
Yoshida, Takashi Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
Yasui, Norihisa Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University ORCID Kaken ID publons
Kusakabe, Yuko Food Research Institute, National Agriculture and Food Research Organization
Ito, Chiaki Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
Akamatsu, Miki Graduate School of Agriculture, Kyoto University
Yamashita, Atsuko Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University Kaken ID publons
抄録
Taste receptor type 1 (T1r) is responsible for the perception of essential nutrients, such as sugars and amino acids, and evoking sweet and umami (savory) taste sensations. T1r receptors recognize many of the taste substances at their extracellular ligand-binding domains (LBDs). In order to detect a wide array of taste substances in the environment, T1r receptors often possess broad ligand specificities. However, the entire ranges of chemical spaces and their binding characteristics to any T1rLBDs have not been extensively analyzed. In this study, we exploited the differential scanning fluorimetry (DSF) to medaka T1r2a/T1r3LBD, a current sole T1rLBD heterodimer amenable for recombinant preparation, and analyzed their thermal stabilization by adding various amino acids. The assay showed that the agonist amino acids induced thermal stabilization and shifted the melting temperatures (T-m) of the protein. An agreement between the DSF results and the previous biophysical assay was observed, suggesting that DSF can detect ligand binding at the orthostericbinding site in T1r2a/T1r3LBD. The assay further demonstrated that most of the tested Lamino acids, but no D-amino acid, induced T-m shifts of T1r2a/T1r3LBD, indicating the broad L-amino acid specificities of the proteins probably with several different manners of recognition. The T-m shifts by each amino acid also showed a fair correlation with the responses exhibited by the full-length receptor, verifying the broad amino-acid binding profiles at the orthosteric site in LBD observed by DSF.
発行日
2019-10-04
出版物タイトル
PLOS ONE
14巻
10号
出版者
Public Library of Science
開始ページ
e0218909
ISSN
1932-6203
資料タイプ
学術雑誌論文
言語
English
OAI-PMH Set
岡山大学
著作権者
© 2019 Yoshida et al.
論文のバージョン
publisher
PubMed ID
DOI
Web of Science KeyUT
関連URL
isVersionOf https://doi.org/10.1371/journal.pone.0218909
ライセンス
https://creativecommons.org/licenses/by/4.0/
助成機関名
日本学術振興会
助成番号
15H05370
17H03644
18H04621