Chimeric Yeast G-Protein Alpha Subunit Harboring a 37-Residue C-Terminal Gustducin-Specific Sequence Is Functional in Saccharomyces cerevisiae

Keisuke HARA; Yuko INADA; Takuya ONO; Kouichi KURODA; Yoshimi YASUDA-KAMATANI; Masaji ISHIGURO; Takaharu TANAKA; Takumi MISAKA; Keiko ABE; Mitsuyoshi UEDA

doi:10.1271/bbb.110820

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Chimeric Yeast G-Protein Alpha Subunit Harboring a 37-Residue C-Terminal Gustducin-Specific Sequence Is Functional in Saccharomyces cerevisiae

Keisuke HARA, Yuko INADA, Takuya ONO, Kouichi KURODA, Yoshimi YASUDA-KAMATANI, Masaji ISHIGURO, Takaharu TANAKA, Takumi MISAKA, Keiko ABE, Mitsuyoshi UEDA

著者情報

キーワード: yeast G-protein-coupled receptor (GPCR) assay, chimeric Gα, G-protein-coupled receptor (GPCR)-Gα interaction, gustducin

ジャーナルフリー早期公開

論文ID: 110820

DOI https://doi.org/10.1271/bbb.110820

この記事には本公開記事があります。

The final version of this article is now available: Vol. 76 (2012) , No. 3 p.512

詳細

抄録

Despite many recent studies of G-protein-coupled receptor (GPCR) structures, it is not yet well understood how these receptors activate G proteins. The GPCR assay using baker’s yeast, Saccharomyces cerevisiae, is an effective experimental model for the characterization of GPCR-Gα interactions. Here, using the yeast endogenous Gα protein (Gpa1p) as template, we constructed various chimeric Gα proteins with a region that is considered to be necessary for interaction with mammalian receptors. The signaling assay using the yeast pheromone receptor revealed that the chimeric Gα protein harboring 37 gustducin-specific amino acid residues at its C-terminus (GPA1/gust37) maintained functionality in yeast. In contrast, GPA1/gust44, a variant routinely used in mammalian experimental systems, was not functional.

責任著者(Corresponding author)

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