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Gene Review

algD  -  GDP-mannose 6-dehydrogenase AlgD

Pseudomonas aeruginosa PAO1

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Disease relevance of algD


High impact information on algD

  • The algU gene is required for expression of the key alginate biosynthetic gene algD and encodes a protein homologous to sigma H, an alternative sigma factor regulating sporulation and other post-exponential-phase processes in Bacillus [6].
  • While the presence of at least one AlgR1 binding site is important for the activation of the algD promoter, the presence of both of the binding sites in the upstream region leads to a higher level of activation [7].
  • The upstream region of the algC gene contained a sequence identical to the algD upstream sequence that is known to be the binding site for the AlgR1 protein [8].
  • The enzyme was overproduced using a plasmid vector containing algD (the gene encoding this enzyme) under control of the tac promoter [9].
  • The subunit molecular weight (Mr 48,000) as well as the N-terminal amino acid sequence corresponded to those predicted from the DNA sequence of algD [9].

Chemical compound and disease context of algD

  • We also demonstrate that the algD promoter is sensitive to glucose repression both in E. coli and P. aeruginosa [3].
  • Gene algD coding for GDPmannose dehydrogenase is transcriptionally activated in mucoid Pseudomonas aeruginosa [10].
  • Pseudomonas aeruginosa produced alginate and elevated algD (encoding GDPmannose 6-dehydrogenase) transcription under strict anaerobic conditions, especially when using nitrate as a terminal electron acceptor [11].
  • Inactivation of Pseudomonas aeruginosa phpA, encoding a putative leucine aminopeptidase, results in increased transcription of algD [12].
  • Pattern of changes in the activity of enzymes of GDP-D-mannuronic acid synthesis and in the level of transcription of algA, algC and algD genes accompanying the loss and emergence of mucoidy in Pseudomonas aeruginosa [13].

Biological context of algD


Associations of algD with chemical compounds

  • Strain PAO1 carried the algD promoter fused to a chloramphenicol acetyl-transferase cartridge (PalgD-cat), and > 50 compounds were tested for promoting chloramphenicol resistance [1].
  • In order to determine whether the alginate or lipopolysaccharide (LPS) defect was responsible for the avirulence of this strain, we constructed a strain with a mutation in an alginate-specific gene, algD [16].
  • Deletion of a putative consensus CRP binding sequence upstream of the algD promoter renders the promoter non-responsive to glucose repression [3].
  • In this report we demonstrate that ethanol (a commonly used dehydrating agent) activates transcription from a critical alginate promoter, algD, and show that prolonged exposure to ethanol allows switching to the mucoid form [17].
  • The response regulators AlgB and AlgR are required for the transcription of algD, a tightly regulated gene encoding GDP-mannose dehydrogenase, which is critical for P. aeruginosa alginate biosynthesis [18].

Physical interactions of algD

  • In gel band mobility shift assays, a protein(s) present in extracts from mucoid and algB and algR mutant P. aeruginosa strains formed a specific complex with algD sequences located immediately upstream of the start of transcription [18].

Regulatory relationships of algD

  • Using the algD-xy1E transcriptional fusion the algD promoter was demonstrated to be under positive control by the algR gene [2].
  • This result suggested that toxA was regulated independently of algD [19].

Other interactions of algD

  • Transcription of algD occurred on the 4th day and increased regularly over time suggesting a balance in the transcription of exoS and algD [20].
  • The algR gene product, which controls transcription of a key alginate biosynthetic gene, algD, is homologous to the activator members of the two-component, environmentally responsive systems (NtrC, OmpR, PhoB, ArcA, etc) [21].
  • Northern blot hybridization experiments also showed that a transposon insertion downstream of algD adversely affected algG and algA transcription [14].
  • We show that algB is transcriptionally active in mucoid strains of P. aeruginosa and regulates the expression of the alginate biosynthetic gene, algD, thereby resulting in increased expression of alginate in mucoid P. aeruginosa [22].
  • When PAO568, a model strain for the analysis of control of the alginate system, was grown under conditions promoting mucoidy, the algD promoter was activated, whereas lasB mRNA could not be detected [23].

Analytical, diagnostic and therapeutic context of algD

  • Electrophoretic mobility-shift assays and copper-phenanthroline footprinting localized AlgZ binding to a 36 bp algD region, which includes several helical repeats [4].
  • This report describes a PCR primer pair that targets the algD GDP mannose gene of Pseudomonas aeruginosa and produces a specific 520-bp PCR product useful for P. aeruginosa identification [24].


  1. Cell wall-inhibitory antibiotics activate the alginate biosynthesis operon in Pseudomonas aeruginosa: roles of sigma (AlgT) and the AlgW and Prc proteases. Wood, L.F., Leech, A.J., Ohman, D.E. Mol. Microbiol. (2006) [Pubmed]
  2. Pseudomonas aeruginosa infection in cystic fibrosis: nucleotide sequence and transcriptional regulation of the algD gene. Deretic, V., Gill, J.F., Chakrabarty, A.M. Nucleic Acids Res. (1987) [Pubmed]
  3. Environmentally regulated algD promoter is responsive to the cAMP receptor protein in Escherichia coli. DeVault, J.D., Hendrickson, W., Kato, J., Chakrabarty, A.M. Mol. Microbiol. (1991) [Pubmed]
  4. Identification and characterization of AlgZ, an AlgT-dependent DNA-binding protein required for Pseudomonas aeruginosa algD transcription. Baynham, P.J., Wozniak, D.J. Mol. Microbiol. (1996) [Pubmed]
  5. Characterization of the gene coding for GDP-mannose dehydrogenase (algD) from Azotobacter vinelandii. Campos, M., Martínez-Salazar, J.M., Lloret, L., Moreno, S., Núñez, C., Espín, G., Soberón-Chávez, G. J. Bacteriol. (1996) [Pubmed]
  6. Mechanism of conversion to mucoidy in Pseudomonas aeruginosa infecting cystic fibrosis patients. Martin, D.W., Schurr, M.J., Mudd, M.H., Govan, J.R., Holloway, B.W., Deretic, V. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  7. Purification of the regulatory protein AlgR1 and its binding in the far upstream region of the algD promoter in Pseudomonas aeruginosa. Kato, J., Chakrabarty, A.M. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  8. Characterization and regulation of the Pseudomonas aeruginosa algC gene encoding phosphomannomutase. Zielinski, N.A., Chakrabarty, A.M., Berry, A. J. Biol. Chem. (1991) [Pubmed]
  9. Purification and characterization of guanosine diphospho-D-mannose dehydrogenase. A key enzyme in the biosynthesis of alginate by Pseudomonas aeruginosa. Roychoudhury, S., May, T.B., Gill, J.F., Singh, S.K., Feingold, D.S., Chakrabarty, A.M. J. Biol. Chem. (1989) [Pubmed]
  10. Gene algD coding for GDPmannose dehydrogenase is transcriptionally activated in mucoid Pseudomonas aeruginosa. Deretic, V., Gill, J.F., Chakrabarty, A.M. J. Bacteriol. (1987) [Pubmed]
  11. Anaerobic production of alginate by Pseudomonas aeruginosa: alginate restricts diffusion of oxygen. Hassett, D.J. J. Bacteriol. (1996) [Pubmed]
  12. Loss of Pseudomonas aeruginosa PhpA aminopeptidase activity results in increased algD transcription. Woolwine, S.C., Sprinkle, A.B., Wozniak, D.J. J. Bacteriol. (2001) [Pubmed]
  13. Pattern of changes in the activity of enzymes of GDP-D-mannuronic acid synthesis and in the level of transcription of algA, algC and algD genes accompanying the loss and emergence of mucoidy in Pseudomonas aeruginosa. Tavares, I.M., Leitão, J.H., Fialho, A.M., Sá-Correia, I. Res. Microbiol. (1999) [Pubmed]
  14. Genetic analysis of the alginate biosynthetic gene cluster of Pseudomonas aeruginosa shows evidence of an operonic structure. Chitnis, C.E., Ohman, D.E. Mol. Microbiol. (1993) [Pubmed]
  15. The roles of mucD and alginate in the virulence of Pseudomonas aeruginosa in plants, nematodes and mice. Yorgey, P., Rahme, L.G., Tan, M.W., Ausubel, F.M. Mol. Microbiol. (2001) [Pubmed]
  16. Avirulence of a Pseudomonas aeruginosa algC mutant in a burned-mouse model of infection. Goldberg, J.B., Coyne, M.J., Neely, A.N., Holder, I.A. Infect. Immun. (1995) [Pubmed]
  17. Pulmonary dehydration and infection in cystic fibrosis: evidence that ethanol activates alginate gene expression and induction of mucoidy in Pseudomonas aeruginosa. DeVault, J.D., Kimbara, K., Chakrabarty, A.M. Mol. Microbiol. (1990) [Pubmed]
  18. Transcriptional analysis of the Pseudomonas aeruginosa genes algR, algB, and algD reveals a hierarchy of alginate gene expression which is modulated by algT. Wozniak, D.J., Ohman, D.E. J. Bacteriol. (1994) [Pubmed]
  19. Positive correlation of algD transcription to lasB and lasA transcription by populations of Pseudomonas aeruginosa in the lungs of patients with cystic fibrosis. Storey, D.G., Ujack, E.E., Mitchell, I., Rabin, H.R. Infect. Immun. (1997) [Pubmed]
  20. Relative expression of Pseudomonas aeruginosa virulence genes analyzed by a real time RT-PCR method during lung infection in rats. Joly, B., Béatrice, J., Pierre, M., Maud, P., Auvin, S., Stéphane, A., Colin, F., Franc Cois, C., Gottrand, F., Frédéric, G., Guery, B., Benoit, G., Husson, M.O. FEMS Microbiol. Lett. (2005) [Pubmed]
  21. Mucoid Pseudomonas aeruginosa in cystic fibrosis: mutations in the muc loci affect transcription of the algR and algD genes in response to environmental stimuli. Deretic, V., Govan, J.R., Konyecsni, W.M., Martin, D.W. Mol. Microbiol. (1990) [Pubmed]
  22. Pseudomonas aeruginosa AlgB, which modulates the expression of alginate, is a member of the NtrC subclass of prokaryotic regulators. Goldberg, J.B., Dahnke, T. Mol. Microbiol. (1992) [Pubmed]
  23. Expression patterns of genes encoding elastase and controlling mucoidy: co-ordinate regulation of two virulence factors in Pseudomonas aeruginosa isolates from cystic fibrosis. Mohr, C.D., Rust, L., Albus, A.M., Iglewski, B.H., Deretic, V. Mol. Microbiol. (1990) [Pubmed]
  24. PCR identification of Pseudomonas aeruginosa and direct detection in clinical samples from cystic fibrosis patients. da Silva Filho, L.V., Levi, J.E., Oda Bento, C.N., da Silva Ramos, S.R., Rozov, T. J. Med. Microbiol. (1999) [Pubmed]
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