Genetic data indicate that proteins containing the GGDEF domain possess diguanylate cyclase activity

FEMS Microbiol Lett. 2001 Oct 16;204(1):163-7. doi: 10.1111/j.1574-6968.2001.tb10880.x.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism
  • Cellulose / metabolism
  • Cyclic GMP / analogs & derivatives*
  • Cyclic GMP / metabolism
  • Escherichia coli Proteins
  • Gene Expression Regulation, Bacterial
  • Phosphorus-Oxygen Lyases / chemistry*
  • Phosphorus-Oxygen Lyases / genetics
  • Phosphorus-Oxygen Lyases / metabolism*
  • Plasmids / genetics
  • Protein Structure, Tertiary
  • Repressor Proteins / chemistry
  • Repressor Proteins / genetics
  • Repressor Proteins / metabolism
  • Rhizobium / enzymology
  • Rhizobium / genetics


  • Bacterial Proteins
  • CelR protein, bacteria
  • Escherichia coli Proteins
  • PleD protein, Caulobacter crescentus
  • Repressor Proteins
  • bis(3',5')-cyclic diguanylic acid
  • Cellulose
  • Phosphorus-Oxygen Lyases
  • diguanylate cyclase
  • Cyclic GMP