Abstract
Dimerization of Nitric Oxide-sensitive Guanylyl Cyclase Requires the α1 N Terminus
Highlights
Most of the effects of the intercellular messenger nitric oxide (NO)1 are mediated by the NO-sensitive guanylyl cyclase (GC) acting as an NO receptor [1, 2]
Dimerization of the ␣ and  subunits is a prerequisite for the functionality of NO-sensitive GC
NO-sensitive GC plays an important role in mammalian cells, as it represents their major NO receptor
Summary
Most of the effects of the intercellular messenger nitric oxide (NO) are mediated by the NO-sensitive guanylyl cyclase (GC) acting as an NO receptor [1, 2]. The ␣11 isoform is considered to be soluble; there is one report on membrane association of the ␣11 enzyme [12]. It represents the predominantly expressed isoform and has been studied intensively by numerous groups. The 1 N terminus has been shown to be responsible for binding of the prosthetic heme group. The catalytic domains are highly conserved between the subunits and are closely related to the catalytic domains of adenylyl cyclases (AC), as shown by the functional expression of AC/GC heterodimers [17]. We identified regions of the subunits of NO-sensitive GC required for dimerization by using deletion mutagenesis. We identified the N-terminal and the central domain of 1 (aa 1–385) to be involved in the respective interaction with ␣1
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