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Willard, F.S. et al.

Purification and in vitro functional analysis of the Arabidopsis thaliana regulator of G-protein signaling-1.

The model organism Arabidopsis thaliana contains a restricted set of heterotrimeric G-protein subunits, with only one canonical Galpha subunit (AtGPA1), one Gbeta subunit (AtAGB1), and two Ggamma subunits (AtAGG1 and AtGG2) identified. We have identified a novel additional component of heterotrimeric G-protein signaling in the A. thaliana genome, regulator of G-protein signaling-1 (AtRGS1). This protein has the predicted topology and structure of a G-protein-coupled receptor in that it contains seven transmembrane domains, but AtRGS1 also contains a unique C-terminal extension, namely a regulator of G-protein signaling domain (RGS box). This article describes methods for the purification and in vitro functional analysis of the RGS box of AtRGS1.[1]

References

Purification and in vitro functional analysis of the Arabidopsis thaliana regulator of G-protein signaling-1. Willard, F.S., Siderovski, D.P. Meth. Enzymol. (2004) [Pubmed]

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