Chimeric yeast G-protein ? subunit harboring a 37-residue C-terminal gustducin-specific sequence is functional in Saccharomyces cerevisiae.

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Chimeric yeast G-protein ? subunit harboring a 37-residue C-terminal gustducin-specific sequence is functional in Saccharomyces cerevisiae.

Biosci Biotechnol Biochem. 2012;76(3):512-6

Authors: Hara K, Inada Y, Ono T, Kuroda K, Yasuda-Kamatani Y, Ishiguro M, Tanaka T, Misaka T, Abe K, Ueda M

Abstract
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-G? interactions. Here, using the yeast endogenous G? protein (Gpa1p) as template, we constructed various chimeric G? 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 G? 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.

PMID: 22451393 [PubMed - indexed for MEDLINE]

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