Multiple active forms of a novel serine protease from Bacillus subtilis

Reinhold Brückner, Oded Shoseyov, Roy H. Doi*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

36 Scopus citations

Abstract

We have cloned and sequenced a gene (epr) encoding a novel serine protease from Bacillus subtilis. Several active forms of the enzyme with molecular masses between 40 and 34 kDa were found in the medium of B. subtilis cultures containing the epr gene cloned on a plasmid. Deletions at the 3′ end of the gene, removing up to 240 amino acids of the reading frame, abolished the expression of the larger species but did not affect the expression of the 34 kDa enzyme. The C-terminal third of the protein is therefore not required for protease activity. The size variation of the active forms expressed by the complete epr gene appears to be the result of partial removal of the C-terminus either by processing or degradation. Thus, the epr gene consists of two domains, one encoding a serine protease homologous to subtilisin and the other a C-terminus of unknown function.

Original languageAmerican English
Pages (from-to)486-490
Number of pages5
JournalZeitschrift fur Vererbungslehre
Volume221
Issue number3
DOIs
StatePublished - May 1990
Externally publishedYes

Keywords

  • C-terminal processing
  • Preproprotein
  • Secretion

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