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

Abstract:

:Calcium-dependent protease (calcium protease) is apparently involved in a variety of cellular processes. 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.

journal_name

Nature

journal_title

Nature

authors

Ohno S,Emori Y,Imajoh S,Kawasaki H,Kisaragi M,Suzuki K

doi

10.1038/312566a0

subject

Has Abstract

pub_date

1984-12-06 00:00:00

pages

566-70

issue

5994

eissn

0028-0836

issn

1476-4687

journal_volume

312

pub_type

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