MsGC-β3 forms active homodimers and inactive heterodimers with NO-sensitive soluble guanylyl cyclase subunits

David Morton, Esther J. Anderson

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

Soluble guanylyl cyclases are typically obligate heterodimers, composed of a single alpha and a single beta subunit. MsGC-β3, 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 β2 subunit also shares this property. Using a combination of gel filtration chromatography, coprecipitation and site-directed mutagenesis we show that, as predicted, MsGC-β3 forms active homodimers. We also demonstrate that MsGC-β3 is capable of forming heterodimers with the nitric oxide (NO)-sensitive guanylyl cyclase subunits MsGC-α1 and MsGC-β1. These heterodimers, however, show no enzyme activity and, like mammalian β2 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-β3 is not necessary for enzyme activity and might act as an auto-inhibitory domain.

Original languageEnglish (US)
Pages (from-to)937-947
Number of pages11
JournalJournal of Experimental Biology
Volume206
Issue number6
DOIs
StatePublished - Mar 2003

Fingerprint

guanylate cyclase
nitric oxide
enzyme activity
Manduca
Manduca sexta
Nitric Oxide
Enzymes
coprecipitation
site-directed mutagenesis
Site-Directed Mutagenesis
tobacco
automobiles
chromatography
Gel Chromatography
gel
Soluble Guanylyl Cyclase

Keywords

  • cGMP
  • Guanylyl cyclase
  • Manduca sexta
  • Nitric oxide
  • Protein dimerization
  • Tobacco hornworm

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Agricultural and Biological Sciences (miscellaneous)

Cite this

MsGC-β3 forms active homodimers and inactive heterodimers with NO-sensitive soluble guanylyl cyclase subunits. / Morton, David; Anderson, Esther J.

In: Journal of Experimental Biology, Vol. 206, No. 6, 03.2003, p. 937-947.

Research output: Contribution to journalArticle

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