Co-Authors:
Tal, R., Cetus Corporation, Emeryville, CA 94608, United States, Sunol Molecular Corporation, Miami, FL 33172, United States
Wong, H.C., Cetus Corporation, Emeryville, CA 94608, United States, Sunol Molecular Corporation, Miami, FL 33172, United States
Calhoon, R., Cetus Corporation, Emeryville, CA 94608, United States
Gelfand, D., Cetus Corporation, Emeryville, CA 94608, United States, Roche Molecular Systems, Emeryville, CA 94608, United States
Fear, A.L., Cetus Corporation, Emeryville, CA 94608, United States, Chiron Corporation, Emeryville, CA 94608, United States
Volman, G., Department of Biological Chemistry, Institute of Life Sciences, Hebrew University of Jerusalem, Jerusalem 91904, Israel
Mayer, R., Department of Biological Chemistry, Institute of Life Sciences, Hebrew University of Jerusalem, Jerusalem 91904, Israel, Department of Agricultural Botany, Faculty of Agriculture, Hebrew University of Jerusalem, Rehovot 76100, Israel
Ross, P., Department of Biological Chemistry, Institute of Life Sciences, Hebrew University of Jerusalem, Jerusalem 91904, Israel
Amikam, D., Department of Biological Chemistry, Institute of Life Sciences, Hebrew University of Jerusalem, Jerusalem 91904, Israel
Weinhouse, H., Department of Biological Chemistry, Institute of Life Sciences, Hebrew University of Jerusalem, Jerusalem 91904, Israel
Cohen, A., Department of Biological Chemistry, Institute of Life Sciences, Hebrew University of Jerusalem, Jerusalem 91904, Israel
Sapir, S., Department of Biological Chemistry, Institute of Life Sciences, Hebrew University of Jerusalem, Jerusalem 91904, Israel
Ohana, P., Department of Biological Chemistry, Institute of Life Sciences, Hebrew University of Jerusalem, Jerusalem 91904, Israel
Benziman, M., Department of Biological Chemistry, Institute of Life Sciences, Hebrew University of Jerusalem, Jerusalem 91904, Israel
Abstract:
Cyclic di-GMP (c-di-GMP) is the specific nucleotide regulator of β- 1,4-glucan (cellulose) synthase in Acetobacterxylinum. 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, and cdg3. Within each cdg operon, a pdeA gene lies upstream of a dgc gene. cdg1 contains two additional flanking genes, cdg1a and cdg1d. cdg1a encodes a putative transcriptional activator, similar to AadR of Rhodopseudomonas 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 the cdg operons, such that cdg1 contributes 80% of cellular DGC and PDEA activities and cdg2 and cdg3 contribute 15 and 5%, respectively. Disruption of dgc genes markedly reduced in vivo cellulose production, demonstrating that c-di-GMP controls this process.
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