Thermo-responsive expression and differential secretion of the extracellular enzyme levansucrase in the plant pathogenic bacterium Pseudomonas syringae pv. glycinea.

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  • Author(s): Li H;Li H; Schenk A; Srivastava A; Zhurina D; Ullrich MS
  • Source:
    FEMS microbiology letters [FEMS Microbiol Lett] 2006 Dec; Vol. 265 (2), pp. 178-85.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Oxford University Press Country of Publication: England NLM ID: 7705721 Publication Model: Print Cited Medium: Print ISSN: 0378-1097 (Print) Linking ISSN: 03781097 NLM ISO Abbreviation: FEMS Microbiol Lett Subsets: MEDLINE
    • Publication Information:
      Publication: 2015- : Oxford Oxford University Press
      Original Publication: Amsterdam, Published by Elsevier/North Holland on behalf of the Federation of European Microbiological Societies.
    • Subject Terms:
      Gene Expression Regulation, Bacterial/*physiology ; Hexosyltransferases/*genetics ; Hexosyltransferases/*metabolism ; Pseudomonas syringae/*enzymology; Blotting, Northern ; Blotting, Western ; Hot Temperature ; Pseudomonas syringae/genetics ; Pseudomonas syringae/pathogenicity ; Glycine max/microbiology
    • Abstract:
      In the plant pathogen Pseudomonas syringae, production of the exopolysaccharide levan is mediated by extracellular levansucrase (Lsc), which is encoded by two functional genes, lscB and lscC. Comparison of extracellular protein profiles of P. syringae pv. glycinea PG4180 grown at 18 and 28 degrees C and Western blots revealed that Lsc was predominantly found in the supernatant at 18 degrees C, a temperature fostering virulence of this pathogen. Northern blot analysis indicated that transcription of lscB and lscC was temperature-dependent. Quantification of Lsc in supernatants and cellular protein samples of mutants defective in either lscB or lscC confirmed that LscB secretion at low temperature was due to a combination of thermo-regulated transcription and secretion. In contrast, LscC accumulated in the periplasmic space. LscB and LscC differ in only five amino acid residues, one of which is a cysteine residue. Temperature shift experiments suggested that de novo synthesized protein(s) at 18 degrees C might be responsible for differential LscB secretion and that the presumed secretory machinery was stable when cells were shifted to 28 degrees C. Our results imply that Lsc export and secretion may occur by yet-to-be identified novel mechanism(s).
    • Accession Number:
      EC 2.4.1.- (Hexosyltransferases)
      EC 2.4.1.10 (levansucrase)
    • Publication Date:
      Date Created: 20061207 Date Completed: 20070226 Latest Revision: 20231213
    • Publication Date:
      20231215
    • Accession Number:
      10.1111/j.1574-6968.2006.00486.x
    • Accession Number:
      17147762