Identification and Modulation of the Key Amino Acid Residue Responsible for the pH Sensitivity of Neoculin, a Taste-Modifying Protein
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{"title"=>"Identification and modulation of the key amino acid residue responsible for the ph sensitivity of neoculin, a taste-modifying protein", "type"=>"journal", "authors"=>[{"first_name"=>"Ken ichiro", "last_name"=>"Nakajima", "scopus_author_id"=>"35080870800"}, {"first_name"=>"Kanako", "last_name"=>"Yokoyama", "scopus_author_id"=>"52165093100"}, {"first_name"=>"Taichi", "last_name"=>"Koizumi", "scopus_author_id"=>"39561322000"}, {"first_name"=>"Ayako", "last_name"=>"Koizumi", "scopus_author_id"=>"8574698200"}, {"first_name"=>"Tomiko", "last_name"=>"Asakura", "scopus_author_id"=>"8589355900"}, {"first_name"=>"Tohru", "last_name"=>"Terada", "scopus_author_id"=>"7202850884"}, {"first_name"=>"Katsuyoshi", "last_name"=>"Masuda", "scopus_author_id"=>"7401446893"}, {"first_name"=>"Keisuke", "last_name"=>"Ito", "scopus_author_id"=>"55478899500"}, {"first_name"=>"Akiko", "last_name"=>"Shimizu-Ibuka", "scopus_author_id"=>"6506900891"}, {"first_name"=>"Takumi", "last_name"=>"Misaka", "scopus_author_id"=>"6602528424"}, {"first_name"=>"Keiko", "last_name"=>"Abe", "scopus_author_id"=>"7404939006"}], "year"=>2011, "source"=>"PLoS ONE", "identifiers"=>{"pui"=>"361731964", "pmid"=>"21559382", "doi"=>"10.1371/journal.pone.0019448", "scopus"=>"2-s2.0-79955755600", "isbn"=>"1932-6203 (Electronic)\\r1932-6203 (Linking)", "issn"=>"19326203", "sgr"=>"79955755600"}, "id"=>"c7bf6108-e658-3fde-9bad-862eafc2fd8c", "abstract"=>"Neoculin occurring in the tropical fruit of Curculigo latifolia is currently the only protein that possesses both a sweet taste and a taste-modifying activity of converting sourness into sweetness. Structurally, this protein is a heterodimer consisting of a neoculin acidic subunit (NAS) and a neoculin basic subunit (NBS). Recently, we found that a neoculin variant in which all five histidine residues are replaced with alanine elicits intense sweetness at both neutral and acidic pH but has no taste-modifying activity. To identify the critical histidine residue(s) responsible for this activity, we produced a series of His-to-Ala neoculin variants and evaluated their sweetness levels using cell-based calcium imaging and a human sensory test. Our results suggest that NBS His11 functions as a primary pH sensor for neoculin to elicit taste modification. Neoculin variants with substitutions other than His-to-Ala were further analyzed to clarify the role of the NBS position 11 in the taste-modifying activity. We found that the aromatic character of the amino acid side chain is necessary to elicit the pH-dependent sweetness. Interestingly, since the His-to-Tyr variant is a novel taste-modifying protein with alternative pH sensitivity, the position 11 in NBS can be critical to modulate the pH-dependent activity of neoculin. These findings are important for understanding the pH-sensitive functional changes in proteinaceous ligands in general and the interaction of taste receptor-taste substance in particular. [ABSTRACT FROM AUTHOR]", "link"=>"http://www.mendeley.com/research/identification-modulation-key-amino-acid-residue-responsible-ph-sensitivity-neoculin-tastemodifying", "reader_count"=>29, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>4, "Researcher"=>5, "Student > Doctoral Student"=>2, "Student > Ph. D. Student"=>3, "Student > Postgraduate"=>1, "Other"=>1, "Student > Master"=>2, "Student > Bachelor"=>7, "Lecturer"=>2, "Lecturer > Senior Lecturer"=>1, "Professor"=>1}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>4, "Researcher"=>5, "Student > Doctoral Student"=>2, "Student > Ph. D. Student"=>3, "Student > Postgraduate"=>1, "Other"=>1, "Student > Master"=>2, "Student > Bachelor"=>7, "Lecturer"=>2, "Lecturer > Senior Lecturer"=>1, "Professor"=>1}, "reader_count_by_subject_area"=>{"Unspecified"=>2, "Engineering"=>1, "Biochemistry, Genetics and Molecular Biology"=>3, "Agricultural and Biological Sciences"=>15, "Medicine and Dentistry"=>3, "Business, Management and Accounting"=>1, "Physics and Astronomy"=>1, "Chemistry"=>2, "Earth and Planetary Sciences"=>1}, "reader_count_by_subdiscipline"=>{"Engineering"=>{"Engineering"=>1}, "Medicine and Dentistry"=>{"Medicine and Dentistry"=>3}, "Chemistry"=>{"Chemistry"=>2}, "Physics and Astronomy"=>{"Physics and Astronomy"=>1}, "Earth and Planetary Sciences"=>{"Earth and Planetary Sciences"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>15}, "Business, Management and Accounting"=>{"Business, Management and Accounting"=>1}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>3}, "Unspecified"=>{"Unspecified"=>2}}, "reader_count_by_country"=>{"Netherlands"=>1, "Denmark"=>1, "United Kingdom"=>1, "Malaysia"=>1}, "group_count"=>2}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/779292"], "description"=>"<p>NAS, NBS, hT1R3, and hT1R2 are colored red, blue, yellow, and orange, respectively. NBS His11 is shown with a green stick model.</p>", "links"=>[], "tags"=>["neoculin", "extracellular", "domains"], "article_id"=>449653, "categories"=>["Biochemistry", "Neuroscience"], "users"=>["Ken-ichiro Nakajima", "Kanako Yokoyama", "Taichi Koizumi", "Ayako Koizumi", "Tomiko Asakura", "Tohru Terada", "Katsuyoshi Masuda", "Keisuke Ito", "Akiko Shimizu-Ibuka", "Takumi Misaka", "Keiko Abe"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0019448.g005", "stats"=>{"downloads"=>2, "page_views"=>13, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Docking_model_of_neoculin_and_the_extracellular_domains_of_human_sweet_taste_receptor_/449653", "title"=>"Docking model of neoculin and the extracellular domains of human sweet taste receptor.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 18:48:02"}
  • {"files"=>["https://ndownloader.figshare.com/files/779176"], "description"=>"<p>(A) Human sensory test of H11X(B) and H11Y/H14A(B) variants. Panelists tasted neoculin variant solutions at pH 7.5 (white) and pH 4.0 (grey) for 15 sec and rated their sweetness levels. Each bar represents the mean ±SD (n = 4–10). The sweetness score was analyzed with a Mann-Whitney <i>U</i>- test (*<i>p</i><0.05). X indicates D, E, F, L, N, R,Q and Y. (B) Far-UV CD spectra of the native neoculin, H11Y(B) and H11Y/H14A(B). The far-UV CD spectra were recorded in 20 mm sodium phosphate buffer, pH 7 or 20 mM sodium citrate buffer, pH 3.0. (C) The pH-dependence of the cell response to neoculin variants. WT neoculin (green), H11A(B) (pink), or H11Y(B) (cyan) (10 µM each) was applied to cells expressing hT1R2-hT1R3 and G15Gi3 under pH 5.5–7.5. The number of responsive cells was normalized relative to the maximum response to aspartame (6.7 mM) at pH 7.4. *<i>p</i><0.05 and **<i>p</i><0.01, one-way ANOVA with Tukey's <i>post hoc</i> test. Each point represents the mean ±SE from three or four independent experiments.</p>", "links"=>[], "tags"=>["ph-dependent"], "article_id"=>449540, "categories"=>["Biochemistry", "Neuroscience"], "users"=>["Ken-ichiro Nakajima", "Kanako Yokoyama", "Taichi Koizumi", "Ayako Koizumi", "Tomiko Asakura", "Tohru Terada", "Katsuyoshi Masuda", "Keisuke Ito", "Akiko Shimizu-Ibuka", "Takumi Misaka", "Keiko Abe"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0019448.g004", "stats"=>{"downloads"=>2, "page_views"=>16, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Modulation_of_the_pH_dependent_activity_of_neoculin_/449540", "title"=>"Modulation of the pH-dependent activity of neoculin.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 18:47:26"}
  • {"files"=>["https://ndownloader.figshare.com/files/778928"], "description"=>"<p>The responses of hT1R2-hT1R3 and G15Gi3 transfected cells were examined after the application of WT neoculin or its single point variants at weakly acidic pH (6.0; closed circle) and at neutral pH (7.5; open circle) and to that of the 5HA variant at neutral pH (7.5; purple circle). A neoculin variant with a His-to-Ala substitution at NBS position 11 is designated H11A(B). The number of responsive cells was normalized relative to the maximum response to aspartame (6.7 mM) at pH 7.4. Each point represents the mean ±SE from three or four independent experiments.</p>", "links"=>[], "tags"=>["relationships", "his-to-ala", "variants", "neoculin", "cell-based"], "article_id"=>449281, "categories"=>["Biochemistry", "Neuroscience"], "users"=>["Ken-ichiro Nakajima", "Kanako Yokoyama", "Taichi Koizumi", "Ayako Koizumi", "Tomiko Asakura", "Tohru Terada", "Katsuyoshi Masuda", "Keisuke Ito", "Akiko Shimizu-Ibuka", "Takumi Misaka", "Keiko Abe"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0019448.g002", "stats"=>{"downloads"=>1, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Dose_response_relationships_of_His_to_Ala_variants_of_neoculin_in_the_cell_based_assay_/449281", "title"=>"Dose-response relationships of His-to-Ala variants of neoculin in the cell-based assay.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 18:46:02"}
  • {"files"=>["https://ndownloader.figshare.com/files/779090"], "description"=>"<p>Panelists tasted His-to-Ala neoculin variant solutions at pH 8.0 (blue), pH 7.5 (red) and pH 4.0 (yellow) for 15 sec and rated their sweetness. Each bar represents the mean ±SD (n = 4–10).</p>", "links"=>[], "tags"=>["sensory", "his-to-ala", "neoculin"], "article_id"=>449450, "categories"=>["Biochemistry", "Neuroscience"], "users"=>["Ken-ichiro Nakajima", "Kanako Yokoyama", "Taichi Koizumi", "Ayako Koizumi", "Tomiko Asakura", "Tohru Terada", "Katsuyoshi Masuda", "Keisuke Ito", "Akiko Shimizu-Ibuka", "Takumi Misaka", "Keiko Abe"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0019448.g003", "stats"=>{"downloads"=>1, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Human_sensory_test_of_His_to_Ala_neoculin_variants_/449450", "title"=>"Human sensory test of His-to-Ala neoculin variants.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 18:46:53"}
  • {"files"=>["https://ndownloader.figshare.com/files/778820"], "description"=>"<p>(A) NAS and NBS are colored red and blue, respectively. His residues are shown with a green stick model. NAS has two His residues at positions 14 and 36. NBS has three His residues at positions 11, 14 and 67. (B) An SDS-PAGE analysis of bacterially produced wild-type neoculin. (C) Far-UV CD spectra of bacterailly produced and native neoculin samples. The far-UV CD spectra were recorded in 20 mm sodium phosphate buffer, pH 7 or 20 mM sodium citrate buffer, pH 3.0.</p>", "links"=>[], "tags"=>["neoculin"], "article_id"=>449167, "categories"=>["Biochemistry", "Neuroscience"], "users"=>["Ken-ichiro Nakajima", "Kanako Yokoyama", "Taichi Koizumi", "Ayako Koizumi", "Tomiko Asakura", "Tohru Terada", "Katsuyoshi Masuda", "Keisuke Ito", "Akiko Shimizu-Ibuka", "Takumi Misaka", "Keiko Abe"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0019448.g001", "stats"=>{"downloads"=>4, "page_views"=>66, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_crystal_structure_of_neoculin_PDB_ID_2D04_/449167", "title"=>"The crystal structure of neoculin (PDB ID: 2D04).", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 18:45:22"}

PMC Usage Stats | Further Information

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