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Revision as of 08:08, 3 October 2017
Sweet Sensing Yeast
Description
Low-caloric artificial sweeteners (LAS) and Low-caloric natural sweeteners (LNS) are among the most widely used food additives worldwide, regularly consumed by lean and obese individuals alike. With the improvement of people's living standard，desired sweeteners are expected far more eagerly due to the growing living level and the developing science technology. The goal of this work is to introduce the human sweet receptor T1R2-T1R3 system to create a practical application of a sweetener sensor using an engineered yeast strain. Initially，we replacing the endogenous yeast G-protein Ste2 with the human sweet receptor T1R2-T1R3, additionally, we deleted some genes to further improve the sensitivity of the T1R2-T1R3 reporter signal. And we also introduce a RFP expression cassette to characterized the relative sweetness degree by RFP fluorescence intensity. Our work will assist the development of a fluorescence-based - sweetening agent sensing system using engineered yeast.
GPCRs constitute the largest family of membrane proteins and are involved in the majority of signal transduction. The common architecture of GPCRs has a seven transmembrane domain structure (Fredriksson et al., 2003; Takeda et al., 2002) that responds to a remarkable range of stimuli, including neurotransmitters, hormones, and ions (Lefkowitz and Shenoy, 2005). G proteins are binary switches that are ‘off’ when bound to guanosine diphosphate (GDP) and ‘on’ when bound to guanosine triphosphate (GTP). The P-loop is responsible for the correct positioning of the triphosphate moiety of the bound nucleotide (M. Saraste,1990). Activation of the G protein stabilises the effector binding site via an interaction with a conserved threonine residue in switch I and a glycine residue in the switch II region, which form hydrogen bonds with the γ-phosphate of GTP in combination with a Mg2+ cofactor. This functionality is conferred by an ∼20 kDa G domain that is conserved across all G proteins .
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