Biophysics and Physicobiology
Online ISSN : 2189-4779
ISSN-L : 2189-4779
Regular Article
Amino acid residues of bitter taste receptor TAS2R16 that determine sensitivity in primates to β-glycosides
Hiroo ImaiNami Suzuki-HashidoYoshiro IshimaruTakanobu SakuraiLijie YinWenshi PanMasaji IshiguroKatsuyoshi MasudaKeiko AbeTakumi MisakaHirohisa Hirai
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Supplementary material

2016 Volume 13 Pages 165-171

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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.

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© 2016 THE BIOPHYSICAL SOCIETY OF JAPAN
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