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Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease and a calcium-binding protein?

Nature volume 312, pages 566–570 (1984)Cite this article

Abstract

Calcium-dependent protease (calcium protease) is apparently involved in a variety of cellular processes1–3. Here we have attempted to clarify the role and regulatory mechanism of calcium protease by analysing its structure. The complete primary structure of calcium protease (relative molecular mass (Mr) 80,000 (80K), 705 amino acids) was deduced from the nucleotide sequence of cloned complementary DNA. The protein contains four distinct domains, and we have observed a marked similarity between the second and fourth domains and the papain-like thiol proteases and calmodulin-like calcium-binding proteins, respectively. This finding suggests that calcium protease arose from the fusion of genes for proteins of completely different function and evolutionary origin. Further, it provides functional insight into cellular regulatory mechanisms mediated by Ca2+ through calcium-binding proteins.

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Authors and Affiliations

  1. Department of Molecular Biology, The Tokyo Metropolitan Institute of Medical Science, 3–18 Honkomagome, Bunkyo-ku, Tokyo, 113, Japan

    Shigeo Ohno, Yasufumi Emori, Shinobu Imajoh, Hiroshi Kawasaki, Masatsugu Kisaragi & Koichi Suzuki

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  1. Shigeo Ohno
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  2. Yasufumi Emori
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  3. Shinobu Imajoh
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  4. Hiroshi Kawasaki
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  5. Masatsugu Kisaragi
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  6. Koichi Suzuki
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Ohno, S., Emori, Y., Imajoh, S. et al. Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease and a calcium-binding protein?. Nature 312, 566–570 (1984). https://doi.org/10.1038/312566a0

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