Multiple active forms of a novel serine protease from Bacillus subtilis

Molecular & General Genetics : MGG
R BrücknerRoy H Doi

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.

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Citations

Sep 1, 1991·Research in Microbiology·X S HeR H Doi
Apr 23, 2003·Biochemical and Biophysical Research Communications·Carsten CorveyKarl-Dieter Entian
Aug 23, 2006·Journal of Bacteriology·Prashant KodgireK Krishnamurthy Rao
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Sep 18, 2004·Journal of Bacteriology·Chi Hye ParkSi Myung Byun
Sep 22, 2007·Journal of Bioscience and Bioengineering·Takeko KodamaJunichi Sekiguchi
Feb 15, 2007·Journal of Bioscience and Bioengineering·Takeko KodamaJunichi Sekiguchi
Dec 15, 2004·Protein Expression and Purification·Chang Won KhoByoung Chul Park
May 7, 2009·FEMS Microbiology Letters·Monica Gupta, Kestur Krishnamurthy Rao
Oct 27, 2015·Applied and Environmental Microbiology·Dongheng MengBing Tang
Oct 15, 2014·Journal of Bacteriology·Rebecca A Calvo, Daniel B Kearns
Apr 22, 2008·FEMS Microbiology Reviews·Lotte P Stenfors ArnesenPer Einar Granum
Oct 24, 2002·Blood·Kenneth G Mann, Michael Kalafatis
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