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Nucleic Acids Research, 1986, Vol. 14, No. 14 5843-5855
© 1986

Articles

Cloning and sequencing of Serratia protease gene

Kazuo Nakahama, Koji Yoshimura, Ryuji Marumoto, Masakazu Kikuchi, In Sook Lee1, Toshiharu Hase1 and Hiroshi Matsubara

Biotechnology Laboratories, Central Research Division, Takeda Chemical Industries, Ltd. Yodogawa-ku, Osaka 532 1Department of Biology, Faculty of Science, Osaka University Toyonaka, Osaka 560, Japan

Received June 17, 1986. Accepted June 30, 1986.

The gene encoding an extracellular metalloproteinase from Serratia sp. E-15 has been cloned, and its complete nucleotide sequence determined. The amino acid sequence deduced from the nucleotide sequence reveals that the mature protein of the Serratia protease consists of 470 amino acids with a molecular weight of 50,632. The G+C content of the coding region for the mature protein is 58%; this high G+C content is due to a marked preference for G+C bases at the third position of the codons. The gene codes for a short pro-peptide preceding the mature protein. The Serratia protease gene was expressed in Escherichia coli and Serratia marcescens; the former produced the Serratia protease in the cells and the latter in the culture medium. Three zinc ligands and an active site of the Serratia protease were predicted by comparing the structure of the enzyme with those of thermolysin and Bacillus subtilis neutral protease.


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