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Extracellular secretion of pectate lyase by the Erwinia chrysanthemi out pathway is dependent upon Sec-mediated export across the inner membrane.

Publication ,  Journal Article
He, SY; Schoedel, C; Chatterjee, AK; Collmer, A
Published in: Journal of bacteriology
July 1991

The plant pathogenic enterobacterium Erwinia chrysanthemi EC16 secretes several extracellular, plant cell wall-degrading enzymes, including pectate lyase isozyme PelE. Secretion kinetics of 35S-labeled PelE indicated that the precursor of PelE was rapidly processed by the removal of the amino-terminal signal peptide and that the resulting mature PelE remained cell bound for less than 60 s before being secreted to the bacterial medium. PelE-PhoA (alkaline phosphatase) hybrid proteins generated in vivo by TnphoA insertions were mostly localized in the periplasm of E. chrysanthemi, and one hybrid protein was observed to be associated with the outer membrane of E. chrysanthemi in an out gene-dependent manner. A gene fusion resulting in the substitution of the beta-lactamase signal peptide for the first six amino acids of the PelE signal peptide did not prevent processing or secretion of PelE in E. chrysanthemi. When pelE was overexpressed, mature PelE protein accumulated in the periplasm rather than the cytoplasm in cells of E. chrysanthemi and Escherichia coli MC4100 (pCPP2006), which harbors a functional cluster of E. chrysanthemi out genes. Removal of the signal peptide from pre-PelE was SecA dependent in E. coli MM52 even in the presence of the out gene cluster. These data indicate that the extracellular secretion of pectic enzymes by E. chrysanthemi is an extension of the Sec-dependent pathway for general export of proteins across the bacterial inner membrane.

Duke Scholars

Published In

Journal of bacteriology

DOI

EISSN

1098-5530

ISSN

0021-9193

Publication Date

July 1991

Volume

173

Issue

14

Start / End Page

4310 / 4317

Related Subject Headings

  • beta-Lactamases
  • SecA Proteins
  • SEC Translocation Channels
  • Restriction Mapping
  • Recombinant Proteins
  • Protein Sorting Signals
  • Polysaccharide-Lyases
  • Plasmids
  • Molecular Sequence Data
  • Microbiology
 

Citation

APA
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ICMJE
MLA
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He, S. Y., Schoedel, C., Chatterjee, A. K., & Collmer, A. (1991). Extracellular secretion of pectate lyase by the Erwinia chrysanthemi out pathway is dependent upon Sec-mediated export across the inner membrane. Journal of Bacteriology, 173(14), 4310–4317. https://doi.org/10.1128/jb.173.14.4310-4317.1991
He, S. Y., C. Schoedel, A. K. Chatterjee, and A. Collmer. “Extracellular secretion of pectate lyase by the Erwinia chrysanthemi out pathway is dependent upon Sec-mediated export across the inner membrane.Journal of Bacteriology 173, no. 14 (July 1991): 4310–17. https://doi.org/10.1128/jb.173.14.4310-4317.1991.
He SY, Schoedel C, Chatterjee AK, Collmer A. Extracellular secretion of pectate lyase by the Erwinia chrysanthemi out pathway is dependent upon Sec-mediated export across the inner membrane. Journal of bacteriology. 1991 Jul;173(14):4310–7.
He, S. Y., et al. “Extracellular secretion of pectate lyase by the Erwinia chrysanthemi out pathway is dependent upon Sec-mediated export across the inner membrane.Journal of Bacteriology, vol. 173, no. 14, July 1991, pp. 4310–17. Epmc, doi:10.1128/jb.173.14.4310-4317.1991.
He SY, Schoedel C, Chatterjee AK, Collmer A. Extracellular secretion of pectate lyase by the Erwinia chrysanthemi out pathway is dependent upon Sec-mediated export across the inner membrane. Journal of bacteriology. 1991 Jul;173(14):4310–4317.

Published In

Journal of bacteriology

DOI

EISSN

1098-5530

ISSN

0021-9193

Publication Date

July 1991

Volume

173

Issue

14

Start / End Page

4310 / 4317

Related Subject Headings

  • beta-Lactamases
  • SecA Proteins
  • SEC Translocation Channels
  • Restriction Mapping
  • Recombinant Proteins
  • Protein Sorting Signals
  • Polysaccharide-Lyases
  • Plasmids
  • Molecular Sequence Data
  • Microbiology