Genetic data indicate that proteins containing the GGDEF domain possess diguanylate cyclase activity
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Updated: Oct 3, 2026

Characterization of G Protein-coupled Receptors by a Fluorescence-based Calcium Mobilization Assay
Published on: July 28, 2014
N Ausmees1, R Mayer, H Weinhouse
1Department of Microbiology, Swedish University of Agricultural Sciences, SLU, Box 7025, S-75007 Uppsala, Sweden. nora.ausmees@mikrob.slu.se
Abstract:
A conserved domain, called GGDEF (referring to a conserved central sequence pattern), is detected in many procaryotic proteins, often in various combinations with putative sensory-regulatory components. Most sequenced bacterial genomes contain several different GGDEF proteins. The function of this domain has so far not been experimentally shown. Through genetic complementation using genes from three different bacteria encoding proteins with GGDEF domains as the only element in common, we present genetic data indicating (a) that the GGDEF domain is responsible for the diguanylate cyclase activity of these proteins, and (b) that the activity of cellulose synthase in Rhizobium leguminosarum bv. trifolii and Agrobacterium tumefaciens is regulated by cyclic di-GMP as in Acetobacter xylinum.
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