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

David P Siderovski, Francis S Willard

Journal: Methods in enzymology 2004;389():320-38

PMID: 15313574

Full Text on Elsevier Science View on PubMed

Abstract

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.

Address: Department of Pharmacology, The University of North Carolina at Chapel Hill, 27599-7365, USA.

DOI: 10.1016/S0076-6879(04)89019-0