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Amino acid residues of bitter taste receptor TAS2R16 that determine sensitivity in primates to β-glycosides
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 duri...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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The Biophysical Society of Japan (BSJ)
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5042178/ https://www.ncbi.nlm.nih.gov/pubmed/27924271 http://dx.doi.org/10.2142/biophysico.13.0_165 |
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author | Imai, Hiroo Suzuki-Hashido, Nami Ishimaru, Yoshiro Sakurai, Takanobu Yin, Lijie Pan, Wenshi Ishiguro, Masaji Masuda, Katsuyoshi Abe, Keiko Misaka, Takumi Hirai, Hirohisa |
author_facet | Imai, Hiroo Suzuki-Hashido, Nami Ishimaru, Yoshiro Sakurai, Takanobu Yin, Lijie Pan, Wenshi Ishiguro, Masaji Masuda, Katsuyoshi Abe, Keiko Misaka, Takumi Hirai, Hirohisa |
author_sort | Imai, Hiroo |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-5042178 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | The Biophysical Society of Japan (BSJ) |
record_format | MEDLINE/PubMed |
spelling | pubmed-50421782016-12-06 Amino acid residues of bitter taste receptor TAS2R16 that determine sensitivity in primates to β-glycosides Imai, Hiroo Suzuki-Hashido, Nami Ishimaru, Yoshiro Sakurai, Takanobu Yin, Lijie Pan, Wenshi Ishiguro, Masaji Masuda, Katsuyoshi Abe, Keiko Misaka, Takumi Hirai, Hirohisa Biophys Physicobiol Regular Article 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. The Biophysical Society of Japan (BSJ) 2016-07-14 /pmc/articles/PMC5042178/ /pubmed/27924271 http://dx.doi.org/10.2142/biophysico.13.0_165 Text en © 2016 The Biophysical Society of Japan This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Regular Article Imai, Hiroo Suzuki-Hashido, Nami Ishimaru, Yoshiro Sakurai, Takanobu Yin, Lijie Pan, Wenshi Ishiguro, Masaji Masuda, Katsuyoshi Abe, Keiko Misaka, Takumi Hirai, Hirohisa Amino acid residues of bitter taste receptor TAS2R16 that determine sensitivity in primates to β-glycosides |
title | Amino acid residues of bitter taste receptor TAS2R16 that determine sensitivity in primates to β-glycosides |
title_full | Amino acid residues of bitter taste receptor TAS2R16 that determine sensitivity in primates to β-glycosides |
title_fullStr | Amino acid residues of bitter taste receptor TAS2R16 that determine sensitivity in primates to β-glycosides |
title_full_unstemmed | Amino acid residues of bitter taste receptor TAS2R16 that determine sensitivity in primates to β-glycosides |
title_short | Amino acid residues of bitter taste receptor TAS2R16 that determine sensitivity in primates to β-glycosides |
title_sort | amino acid residues of bitter taste receptor tas2r16 that determine sensitivity in primates to β-glycosides |
topic | Regular Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5042178/ https://www.ncbi.nlm.nih.gov/pubmed/27924271 http://dx.doi.org/10.2142/biophysico.13.0_165 |
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