Evolution of the EF-hand calcium-binding protein family: Evidence for exon shuffling and intron insertion
- 1 August 1988
- journal article
- research article
- Published by Springer Nature in Journal of Molecular Evolution
- Vol. 27 (4) , 351-364
- https://doi.org/10.1007/bf02101198
Abstract
The evolutionary history of the intracellular calcium-binding protein superfamily is well documented. The members of this gene family are all believed to be derived from a common ancestor, which, itself, was the product of two successive gene duplications. In this study, we have compared and analyzed the structures of the recently described genes coding for these proteins. We propose a series of evolutionary events, which include exon shuffling and intron insertion, that could account for the evolutionary origin of all the members of this super-family. According to this hypothesis, the ancestral gene, a product of two successive duplications, consisted of at least four exons. Each exon coding for a peptide (a calcium-binding domain) was separated by an intron that had mediated the duplication. Each distinct lineage evolved from this ancestor by genomic rearrangement, with insertion of introns being a prominent feature.Keywords
This publication has 84 references indexed in Scilit:
- Structure of a gene for rat calmodulinJournal of Molecular Biology, 1987
- A novel calmodulin-like gene from the nematode Caenorhabditis elegansJournal of Molecular Biology, 1986
- Amino acid sequence of vitamin D‐dependent calcium‐binding protein from bovine cerebellumFEBS Letters, 1986
- Gene structure of calcium‐dependent protease retains the ancestral organization of the calcium‐binding protein geneFEBS Letters, 1986
- Structure of the Spec1 gene encoding a major calcium-binding protein in the embryonic ectoderm of the sea urchin, Strongylocentrotus purpuratusJournal of Molecular Biology, 1985
- Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modulesCell, 1985
- Molecular evolution of proteinJournal of Molecular Biology, 1982
- Evolutionary diversification of structure and function in the family of intracellular calcium-binding proteinsJournal of Molecular Evolution, 1979
- Refinement of the structure of carp muscle calcium-binding parvalbumin by model building and difference fourier analysisJournal of Molecular Biology, 1975
- Structural homology of myosin alkali light chains, troponin C and carp calcium binding proteinNature, 1974