Secretion of methanol-insoluble heat-stable enterotoxin (ST(B))

Energy- and secA-dependent conversion of Pre-ST(B) to an intermediate indistinguishable from the extracellular toxin

Y. M. Kupersztoch, K. Tachias, C. R. Moomaw, L. A. Dreyfus, R. Urban, Clive A. Slaughter, S. Whipp

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

The methanol-insoluble, heat-stable enterotoxin of Escherichia coli synthesized by clinical strains or strains that harbor the cloned gene was shown to be an extracellular polypeptide. The toxin (ST(B)) was first detected as an 8,100-M(r) precursor (pre-ST(B)) that was converted to a transiently cell-associated 5,200-M(r) form. Proteolytic conversion of pre-ST(B) to ST(B) was shown to be inhibited by the proton motive force uncoupler carbonyl cyanide m-chlorophenylhydrazone and did not occur in a secA background. After ST(B) was detected as a cell-associated molecule, an extracellular form with identical electrophoretic mobility became apparent. The results suggest that there is no proteolytic processing during the mobilization of ST(B) from the periplasm to the culture supernatant. The determined amino acid sequence of ST(B) coincides fully with the 48 carboxy-terminal amino acids inferred from the DNA sequence. The 23 amino-terminal residues inferred from the DNA sequence were absent in the mature toxin.

Original languageEnglish (US)
Pages (from-to)2427-2432
Number of pages6
JournalJournal of Bacteriology
Volume172
Issue number5
DOIs
StatePublished - Jan 1 1990
Externally publishedYes

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Methanol
Hot Temperature
Periplasm
Proton-Motive Force
Enterotoxins
Amino Acid Sequence
Escherichia coli
Amino Acids
Peptides
Genes
heat stable toxin (E coli)
mesoxalonitrile
carbonyl 3-chlorophenylhydrazone

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

Cite this

Secretion of methanol-insoluble heat-stable enterotoxin (ST(B)) : Energy- and secA-dependent conversion of Pre-ST(B) to an intermediate indistinguishable from the extracellular toxin. / Kupersztoch, Y. M.; Tachias, K.; Moomaw, C. R.; Dreyfus, L. A.; Urban, R.; Slaughter, Clive A.; Whipp, S.

In: Journal of Bacteriology, Vol. 172, No. 5, 01.01.1990, p. 2427-2432.

Research output: Contribution to journalArticle

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abstract = "The methanol-insoluble, heat-stable enterotoxin of Escherichia coli synthesized by clinical strains or strains that harbor the cloned gene was shown to be an extracellular polypeptide. The toxin (ST(B)) was first detected as an 8,100-M(r) precursor (pre-ST(B)) that was converted to a transiently cell-associated 5,200-M(r) form. Proteolytic conversion of pre-ST(B) to ST(B) was shown to be inhibited by the proton motive force uncoupler carbonyl cyanide m-chlorophenylhydrazone and did not occur in a secA background. After ST(B) was detected as a cell-associated molecule, an extracellular form with identical electrophoretic mobility became apparent. The results suggest that there is no proteolytic processing during the mobilization of ST(B) from the periplasm to the culture supernatant. The determined amino acid sequence of ST(B) coincides fully with the 48 carboxy-terminal amino acids inferred from the DNA sequence. The 23 amino-terminal residues inferred from the DNA sequence were absent in the mature toxin.",
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AU - Urban, R.

AU - Slaughter, Clive A.

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N2 - The methanol-insoluble, heat-stable enterotoxin of Escherichia coli synthesized by clinical strains or strains that harbor the cloned gene was shown to be an extracellular polypeptide. The toxin (ST(B)) was first detected as an 8,100-M(r) precursor (pre-ST(B)) that was converted to a transiently cell-associated 5,200-M(r) form. Proteolytic conversion of pre-ST(B) to ST(B) was shown to be inhibited by the proton motive force uncoupler carbonyl cyanide m-chlorophenylhydrazone and did not occur in a secA background. After ST(B) was detected as a cell-associated molecule, an extracellular form with identical electrophoretic mobility became apparent. The results suggest that there is no proteolytic processing during the mobilization of ST(B) from the periplasm to the culture supernatant. The determined amino acid sequence of ST(B) coincides fully with the 48 carboxy-terminal amino acids inferred from the DNA sequence. The 23 amino-terminal residues inferred from the DNA sequence were absent in the mature toxin.

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