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Nucleic Acids Research, 1985, Vol. 13, No. 24 8913-8926
© 1985

Articles

Cloning, sequencing and expression of subtilisin Carlsberg from Bacillus licheniformis

Myra Jacobs1, Margareta Eliasson2, Mathias Uhlén2,3,4,* and Jan-Ingmar Flock4

1Novo Research Institute Novo Alle, DK-2880 Bagsvaerd, Denmark 2Department of Biochemistry, Royal Institute of Technology S-100 44 Stockholm, Sweden 3European Molecular Biology Laboratory Postfach 10.2209, D-6900 Heidelberg, FRG 4Department of Microbiology, The Biomedical Center Box 581, S-751 23 Uppsala, Sweden

*To whom correspondence should be addressed at: European Molecular Biology Laboratory, Postfach 10.2209, D-6900 Heidelberg, FRG

Received October 11, 1985. Revised November 6, 1985. Accepted November 22, 1985.

The gene encoding subtilisin Carlsberg from Bacillus licheniformis has been isolated by molecular cloning using a mixture of synthetic oligonucleotides. The entire nucleotide sequence of the coding sequence as well as 5' and 3' flanking sequences have been determined. The deduced amino acid sequence reveals an N-terminal signal peptide consisting of 29 residues, a pro-peptide of 76 residues followed by the mature protein comprising 274 residues. The ATG initiator codon is proceeded by two putitative overlapping ribosomal binding sequences. A palindromic sequence typical for transcription termination is found downstream from the TAA stop codon. Structural comparisons between different known subtilisin genes reveal extensive homology, particularly in the parts coding for the pro-region and the mature protein. Expression studies in Bacillus subtilis show that the cloned fragment produces a functional enzyme when inserted after a B. subtilis promoter.


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