TY - JOUR
T1 - Purification and in vitro functional analysis of the Arabidopsis thaliana regulator of G-protein signaling-1
AU - Willard, Francis S.
AU - Siderovski, David P.
N1 - Funding Information:
We thank Dr. Martin R. Webb (National Institute of Medical Research, Mill Hill, UK) for provision of the PBP expression construct and Drs. Adam Shutes (UNC) and Krister Wennerburg (UNC) for assistance with the production of MDCC-PBP. Thanks also to Dr. Alan Jones (UNC) for the construct pDEST15-AtRGS1(249–459) and the UNC Department of Pharmacology Protein Core for provision of instrumentation. FSW is an American Heart Association Postdoctoral Fellow. This work was funded by NIH Grants R01 GM062338 and P01 GM065533. DPS is a recipient of the Burroughs Wellcome Fund New Investigator Award in the Pharmacological Sciences.
PY - 2004
Y1 - 2004
N2 - The model organism Arabidopsis thaliana contains a restricted set of heterotrimeric G-protein subunits, with only one canonical Gα subunit (AtGPA1), one Gβ subunit (AtAGB1), and two Gγ 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.
AB - The model organism Arabidopsis thaliana contains a restricted set of heterotrimeric G-protein subunits, with only one canonical Gα subunit (AtGPA1), one Gβ subunit (AtAGB1), and two Gγ 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.
UR - http://www.scopus.com/inward/record.url?scp=4344670030&partnerID=8YFLogxK
U2 - 10.1016/S0076-6879(04)89019-0
DO - 10.1016/S0076-6879(04)89019-0
M3 - Article
C2 - 15313574
AN - SCOPUS:4344670030
SN - 0076-6879
VL - 389
SP - 320
EP - 338
JO - Methods in Enzymology
JF - Methods in Enzymology
ER -