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The Journal of Experimental Biology 206, 937-947 (2003)
doi: 10.1242/jeb.00160

MsGC-ß3 forms active homodimers and inactive heterodimers with NO-sensitive soluble guanylyl cyclase subunits

David B. Morton^* and Esther J. Anderson

Department of Biological Structure and Function, Oregon Health and Science University, Portland, Oregon, USA

^* Author for correspondence (e-mail: mortonda{at}ohsu.edu)

Accepted 20 December 2002

Soluble guanylyl cyclases are typically obligate heterodimers, composed of a single alpha and a single beta subunit. MsGC-ß3, identified in the tobacco hornworm Manduca sexta, was the first example of a soluble guanylyl cyclase that exhibited enzyme activity without the need for coexpression with additional subunits. Subsequent studies have revealed that the mammalian ß2 subunit also shares this property. Using a combination of gel filtration chromatography, coprecipitation and site-directed mutagenesis we show that, as predicted, MsGC-ß3 forms active homodimers. We also demonstrate that MsGC-ß3 is capable of forming heterodimers with the nitric oxide (NO)-sensitive guanylyl cyclase subunits MsGC-1 and MsGC-ß1. These heterodimers, however, show no enzyme activity and, like mammalian ß2 subunits, act in a dominant negative manner when combined with the NO-sensitive subunits to disrupt their activation by NO. In addition, we show that the unique C-terminal domain of MsGC-ß3 is not necessary for enzyme activity and might act as an auto-inhibitory domain.

Key words: cGMP, guanylyl cyclase, nitric oxide, protein dimerization, tobacco hornworm, Manduca sexta

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