This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Zhang, J. H.
Right arrow Articles by Gross, D. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zhang, J. H.
Right arrow Articles by Gross, D. C.
Agricola
Right arrow Articles by Zhang, J. H.
Right arrow Articles by Gross, D. C.

 Previous Article  |  Next Article 

Appl. Environ. Microbiol., 07 1997, 2771-2778, Vol 63, No. 7
Copyright © 1997, American Society for Microbiology

Analysis of the syrP gene, which regulates syringomycin synthesis by Pseudomonas syringae pv. syringae

JH Zhang, NB Quigley and DC Gross
Department of Plant Pathology, Washington State University, Pullman 99164-6430, USA.

Syringomycin is a lipodepsinonapeptide phytotoxin synthesized by Pseudomonas syringae pv. syringae on multienzymatic peptide synthetases. Sequence analysis of the interval between the syrB and syrD genes of P. syringae pv. syringae strain B301D revealed a 1,059-bp open reading frame (ORF), designated syrP. The predicted product of this ORF was a 39.6-kDa protein consisting of 353 amino acid residues. Searches of protein sequence databases demonstrated that SyrP was most similar to histidine kinases such as the CheA regulatory protein of Escherichia coli. The predicted SyrP sequence was aligned with the N terminus of CheA, a region corresponding to the phosphotransfer and acceptor domains of CheA. The SyrP region that aligns with the phosphotransfer domain of CheA contained a His at position 101 which is flanked by a weak consensus sequence of the unorthodox sensory kinase subfamily of two-component regulatory systems. Strain B301D-31, obtained by site-directed insertional mutagenesis of the syrP gene, exhibited an unusual pleiotropic phenotype including a failure to produce syringomycin in liquid media in contrast to production of elevated levels of the toxin on agar media. The syrP mutant was relieved of the suppression of toxin production that accompanies inorganic phosphate concentrations of > 1 mM on agar media. Nevertheless, the syrP mutant was substantially less virulent than the wild-type strain in pathogenicity assays in cherry fruits. These results suggest that the syrP gene encodes a regulatory protein that participates in a phosphorylation cascade controlling syringomycin production and virulence in P. syringae pv. syringae.


This article has been cited by other articles:

  • Muller, C., Nolden, S., Gebhardt, P., Heinzelmann, E., Lange, C., Puk, O., Welzel, K., Wohlleben, W., Schwartz, D. (2007). Sequencing and Analysis of the Biosynthetic Gene Cluster of the Lipopeptide Antibiotic Friulimicin in Actinoplanes friuliensis. Antimicrob. Agents Chemother. 51: 1028-1037 [Abstract] [Full Text]  
  • Wang, N., Lu, S.-E., Records, A. R., Gross, D. C. (2006). Characterization of the Transcriptional Activators SalA and SyrF, Which Are Required for Syringomycin and Syringopeptin Production by Pseudomonas syringae pv. syringae. J. Bacteriol. 188: 3290-3298 [Abstract] [Full Text]  
  • Vaillancourt, F. H., Yin, J., Walsh, C. T. (2005). From The Cover: SyrB2 in syringomycin E biosynthesis is a nonheme FeII {alpha}-ketoglutarate- and O2-dependent halogenase. Proc. Natl. Acad. Sci. USA 102: 10111-10116 [Abstract] [Full Text]  
  • Wu, G., Culley, D. E., Zhang, W. (2005). Predicted highly expressed genes in the genomes of Streptomyces coelicolor and Streptomyces avermitilis and the implications for their metabolism. Microbiology 151: 2175-2187 [Abstract] [Full Text]  
  • Brencic, A., Winans, S. C. (2005). Detection of and Response to Signals Involved in Host-Microbe Interactions by Plant-Associated Bacteria. Microbiol. Mol. Biol. Rev. 69: 155-194 [Abstract] [Full Text]  
  • Lu, S.-E., Soule, J. D., Gross, D. C. (2003). Characterization of the argA Gene Required for Arginine Biosynthesis and Syringomycin Production by Pseudomonas syringae pv. syringae. Appl. Environ. Microbiol. 69: 7273-7280 [Abstract] [Full Text]  
  • Heinzelmann, E., Berger, S., Puk, O., Reichenstein, B., Wohlleben, W., Schwartz, D. (2003). A Glutamate Mutase Is Involved in the Biosynthesis of the Lipopeptide Antibiotic Friulimicin in Actinoplanes friuliensis. Antimicrob. Agents Chemother. 47: 447-457 [Abstract] [Full Text]  
  • Bender, C. L., Alarcon-Chaidez, F., Gross, D. C. (1999). Pseudomonas syringae Phytotoxins: Mode of Action, Regulation, and Biosynthesis by Peptide and Polyketide Synthetases. Microbiol. Mol. Biol. Rev. 63: 266-292 [Abstract] [Full Text]  
  • Bultreys, A., Gheysen, I. (1999). Biological and Molecular Detection of Toxic Lipodepsipeptide-Producing Pseudomonas syringae Strains and PCR Identification in Plants. Appl. Environ. Microbiol. 65: 1904-1909 [Abstract] [Full Text]  
  • Guenzi, E., Galli, G., Grgurina, I., Gross, D. C., Grandi, G. (1998). Characterization of the Syringomycin Synthetase Gene Cluster. A LINK BETWEEN PROKARYOTIC AND EUKARYOTIC PEPTIDE SYNTHETASES. J. Biol. Chem. 273: 32857-32863 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»