-
Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease and a calcium-binding protein?
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.
PMID: 6095110 [PubMed - indexed for MEDLINE]
-
Cited by 44 PubMed Central articles
-
ReviewNeuroprotection in glaucoma using calpain-1 inhibitors: regional differences in calpain-1 activity in the trabecular meshwork, optic nerve and implications for therapeutics.
Govindarajan B, Laird J, Sherman R, Salomon RG, Bhattacharya SK.
CNS Neurol Disord Drug Targets. 2008 Jun; 7(3):295-304.
[CNS Neurol Disord Drug Targets. 2008]
-
Analysis of mRNAs that Accumulate in Response to Low Temperature Identifies a Thiol Protease Gene in Tomato.
Schaffer MA, Fischer RL.
Plant Physiol. 1988 Jun; 87(2):431-436.
[Plant Physiol. 1988]
-
Disruption of the murine calpain small subunit gene, Capn4: calpain is essential for embryonic development but not for cell growth and division.
Arthur JS, Elce JS, Hegadorn C, Williams K, Greer PA.
Mol Cell Biol. 2000 Jun; 20(12):4474-81.
[Mol Cell Biol. 2000]
- » See all...