Amino acid residues of bitter taste receptor TAS2R16 that determine sensitivity in primates to β-glycosides

• Imai Hiroo

  Primate Research Institute, Kyoto University

• Suzuki-Hashido Nami

  Primate Research Institute, Kyoto University

• Ishimaru Yoshiro

  Graduate School of Agricultural and Life Sciences, The University of Tokyo

• Sakurai Takanobu

  Graduate School of Agricultural and Life Sciences, The University of Tokyo

• Yin Lijie

  Center for Nature and Society, School of Life Sciences, Peking University

• Pan Wenshi

  Center for Nature and Society, School of Life Sciences, Peking University

• Ishiguro Masaji

  Department of Applied Life Sciences, Niigata University of Pharmacy and Applied Life Sciences

• Masuda Katsuyoshi

  Suntory Institute for Bioorganic Research

• Abe Keiko

  Graduate School of Agricultural and Life Sciences, The University of Tokyo

• Misaka Takumi

  Graduate School of Agricultural and Life Sciences, The University of Tokyo

• Hirai Hirohisa

  Primate Research Institute, Kyoto University

Abstract

In mammals, bitter taste is mediated by TAS2Rs, which belong to the family of seven transmembrane G protein-coupled receptors. Since TAS2Rs are directly involved in the interaction between mammals and their dietary sources, it is likely that these genes evolved to reflect species-specific diets during mammalian evolution. Here, we analyzed the amino acids responsible for the difference in sensitivities of TAS2R16s of various primates using a cultured cell expression system. We found that the sensitivity of TAS2R16 varied due to several amino acid residues. Mutation of amino acid residues at E86T, L247M, and V260F in human and langur TAS2R16 for mimicking the macaque TAS2R16 decreased the sensitivity of the receptor in an additive manner, which suggests its contribution to the potency of salicin, possibly via direct interaction. However, mutation of amino acid residues 125 and 133 in human TAS2R16, which are situated in helix 4, to the macaque sequence increased the sensitivity of the receptor. These results suggest the possibility that bitter taste sensitivities evolved independently by replacing specific amino acid residues of TAS2Rs in different primate species to adapt to species-specific food.

Journal

• Biophysics and Physicobiology

  Biophysics and Physicobiology 13 (0), 165-171, 2016

  The Biophysical Society of Japan

Keywords

• cell signaling
• molecular evolution
• G protein-coupled receptor
• receptor regulation
• primates
• bitter taste

Details

• CRID: 1390001205763061632
• NII Article ID: 130005165371
• DOI: 10.2142/biophysico.13.0_165
• ISSN: 21894779
• Web Site: https://www.jstage.jst.go.jp/article/biophysico/13/0/13_165/_pdf
• Text Lang: en
• Data Source:
  • JaLC
  • Crossref
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed