Production of active Serratia marcescens metalloprotease from Escherichia coli by α-hemolysin HlyB and HlyD

Yousin Suh, M. J. Benedik

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

Serratia marcescens produces an abundant extracellular metalloprotease. The gene for this protease had previously been cloned and expressed in Escherichia coli, in which no functional protease could be found. However, the protease gene carries the LXGGXGND repeat motif found in α-hemolysin and other proteins secreted by homologous systems. Using a dual-plasmid complementation system, we show that the α-hemolysin hlyB and hlyD transport determinants are sufficient to allow secretion and activation of a functional metalloprotease species from E. coli, as are the comparable protease secretion functions of Erwinia chrysanthemi. However, strains expressing protease with the hlyBD transport system are unstable and rapidly lose the ability to produce functional protease.

Original languageEnglish (US)
Pages (from-to)2361-2366
Number of pages6
JournalJournal of Bacteriology
Volume174
Issue number7
StatePublished - 1992
Externally publishedYes

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Serratia marcescens
Hemolysin Proteins
Metalloproteases
Peptide Hydrolases
Escherichia coli
Pectobacterium chrysanthemi
Genes
Plasmids

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

Cite this

Production of active Serratia marcescens metalloprotease from Escherichia coli by α-hemolysin HlyB and HlyD. / Suh, Yousin; Benedik, M. J.

In: Journal of Bacteriology, Vol. 174, No. 7, 1992, p. 2361-2366.

Research output: Contribution to journalArticle

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