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Molecular evolution of group II phospholipases A2
T Ogawa1, M Kitajima, K Nakashima
1Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka, Japan.
Journal of Molecular Evolution
|December 1, 1995
Summary
Phylogenetic analysis of group II phospholipase A2 (PLA2) genes reveals distinct evolutionary patterns. Snake venom PLA2 genes show accelerated evolution, differing from mammalian PLA2 genes, leading to diverse activities.
Area of Science:
- Molecular Evolution
- Genomics
- Biochemistry
Background:
- Group II phospholipases A2 (PLA2s) are enzymes found in snake venoms and mammalian tissues.
- Understanding the evolutionary divergence of PLA2 genes is crucial for deciphering their diverse physiological roles.
Purpose of the Study:
- To analyze the evolutionary pathways of group II PLA2 genes from viperidae snakes and mammalian sources.
- To investigate the distinct evolutionary pressures acting on different regions of PLA2 cDNAs.
Main Methods:
- Phylogenetic tree construction using nucleotide sequences of 13 group II PLA2 cDNAs.
- Analysis of untranslated regions, signal peptide regions, and mature protein-coding regions.
- Comparison of evolutionary patterns between snake venom and mammalian PLA2 genes.
Main Results:
- Evolutionary trees from untranslated and signal peptide regions aligned with taxonomic classifications.
- Evolutionary trees from mature protein-coding regions and amino acid sequences showed random patterns, indicating different evolutionary processes.
- Phylogenetic analysis suggests snake venom PLA2 genes evolved via accelerated evolution, distinct from mammalian PLA2 genes.
Conclusions:
- The mature protein-coding region of PLA2 genes evolves differently from untranslated and signal peptide regions.
- Accelerated evolution in snake venom group II PLA2 isozyme genes contributes to their diverse physiological activities.
- This study provides further evidence for accelerated evolution in snake venom PLA2 isozyme genes.