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Cyclic di-GMP (c-di-GMP) is the specific nucleotide regulator of β-1,4-glucan (cellulose) synthase inAcetobacter xylinum . The enzymes controlling turnover of c-di-GMP are diguanylate cyclase (DGC), which catalyzes its formation, and phosphodiesterase A (PDEA), which catalyzes its degradation. Following biochemical purification of DGC and PDEA, genes encoding isoforms of these enzymes have been isolated and found to be located on three distinct yet highly homologous operons for cyclic diguanylate,cdg1 ,cdg2 , andcdg3 . Within eachcdg operon, apdeA gene lies upstream of adgc gene.cdg1 contains two additional flanking genes,cdg1a andcdg1d. cdg1a encodes a putative transcriptional activator, similar to AadR ofRhodopseudomonas palustris and FixK proteins of rhizobia. The deduced DGC and PDEA proteins have an identical motif structure of two lengthy domains in their C-terminal regions. These domains are also present in numerous bacterial proteins of undefined function. The N termini of the DGC and PDEA deduced proteins contain putative oxygen-sensing domains, based on similarity to domains on bacterial NifL and FixL proteins, respectively. Genetic disruption analyses demonstrated a physiological hierarchy among thecdg operons, such thatcdg1 contributes 80% of cellular DGC and PDEA activities andcdg2 andcdg3 contribute 15 and 5%, respectively. Disruption ofdgc genes markedly reduced in vivo cellulose production, demonstrating that c-di-GMP controls this process.

journal of bacteriology

Three <i>cdg</i> Operons Control Cellular Turnover of Cyclic Di-GMP in <i>Acetobacter xylinum</i> : Genetic Organization and Occurrence of Conserved Domains in Isoenzymes

Three cdg Operons Control Cellular Turnover of Cyclic Di-GMP in Acetobacter xylinum : Genetic Organization and Occurrence of Conserved Domains in Isoenzymes