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J Biol Chem, Vol. 274, Issue 26, 18149-18152, June 25, 1999

COMMUNICATION
Homodimerization of Soluble Guanylyl Cyclase Subunits
DIMERIZATION ANALYSIS USING A GLUTATHIONE S-TRANSFERASE AFFINITY TAG

From the Department of Pharmacology and Toxicology, Julius-Maximilians-University, D-97078 Wuerzburg, Germany

Soluble guanylyl cyclase (sGC) is an /-heterodimeric hemoprotein that, upon interaction with the intercellular messenger molecule NO, generates cGMP. Although the related family of particulate guanylyl cyclases (pGCs) forms active homodimeric complexes, it is not known whether homodimerization of sGC subunits occurs. We report here the expression in Sf9 cells of glutathione S-transferase-tagged recombinant human sGC1 and 1 subunits, applying a novel and rapid purification method based on GSH-Sepharose affinity chromatography. Surprisingly, in intact Sf9 cells, both homodimeric GST/ and GST/ complexes were formed that were catalytically inactive. Upon coexpression of the respective complementary subunits, GST/ or GST/ heterodimers were preferentially formed, whereas homodimers were still detectable. When subunits were mixed after expression, e.g. GST and  or GST and , no dimerization was observed. In conclusion, our data suggest the previously unrecognized possibility of a physiological equilibrium between homo- and heterodimeric sGC complexes.

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