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Volume 271, Number 47, Issue of November 22, 1996 pp. 29521-29524
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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COMMUNICATION:
Molecular Cloning of Manganese Catalase from Lactobacillus plantarum

(Received for publication, September 9, 1996)

Takao Igarashi , Yasuhisa Kono ^¶ and Kiyoshi Tanaka

From the  Environmental Biology Division, National Institute for Environmental Studies, Onogawa, Tsukuba, Ibaraki 305, Japan, the ^¶ Department of Life Science and Biotechnology, Faculty of Life and Environmental Science, Shimane University, Matsue, Shimane 690, Japan, and the  Laboratory of Plant Biotechnology, Department of Biochemistry and Biotechnology, Faculty of Agriculture, Tottori University, Koyama, Tottori 680, Japan

A genomic clone encoding manganese-containing catalase has been isolated from lactic acid bacterium Lactobacillus plantarum, sequenced, and expressed in Escherichia coli cells with an inducible expression system. The primary structure of the enzyme deduced from the nucleotide sequence, that comprises 266 amino acid residues, showed no significant homology with that of any other proteins registered on the available data bases. No peptide motifs conserved among active sites of proteins including manganese-containing enzymes were found. The E. coli cells carrying an expression construct, in which the 5-noncoding region of the manganese catalase gene was replaced with the lac promoter, highly induced a protein reacting with the antiserum to manganese catalase.

The prediction of secondary structure from the deduced primary structure suggested that the L. plantarum manganese catalase, that is classified as a novel protein on the basis of its primary structure, has a main structural motif formed by four near parallel helices between which is the catalytic site manganese.

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