Signal peptidase cleavage site in the processing of Pseudomonas aeruginosa preproelastase

Yuji Shibano, Kenji Inagaki, Jun Fukushima, Susumu Kawamoto, Kenji Okuda, Kazuyuki Morihara

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

The extracellular elastase (33 kDa) of Pseudomonas aeruginosa is synthesized as a 53.6-kDa preproenzyme containing a long N-terminal propeptide, which is processed to the mature form via a 51-kDa proelastase. A 51-kDa protein isolated from Escherichia coli transformant carrying the Glu141→Gln mutant elastase gene was subjected to N-terminal amino acid sequence analysis. No autoproteolytic processing of proelastase was expected to occur in these cells. The data indicated that the N-terminal sequence corresponds to the position between -174 and -164 of the preproelastase (numbers are in reference to the first amino acid residue of mature elastase). This confirms that the 51-kDa protein is proelastase and that the signal peptidase cleaves between Ala-175 and Ala-174.

Original languageEnglish
Pages (from-to)331-332
Number of pages2
JournalJournal of Fermentation and Bioengineering
Volume78
Issue number4
DOIs
Publication statusPublished - 1994

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology

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