𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Molecular evolution of group II phospholipases A2

✍ Scribed by Tomohisa Ogawa; Masato Kitajima; Kin-ichi Nakashima; Yoshiyuki Sakaki; Motonori Ohno


Publisher
Springer
Year
1995
Tongue
English
Weight
854 KB
Volume
41
Category
Article
ISSN
0022-2844

No coin nor oath required. For personal study only.

✦ Synopsis


The nucleotide sequences of 13 cDNAs encoding group II phospholipases A2 (PLA2s), which are from viperidae snake venoms and from mammalian sources, were aligned and analyzed by phylogenetic trees constructed using various components of the sequences. The evolutionary trees derived from the combined sequences of the untranslated (5' and 3') region and the signal peptide region of cDNAs were in accord with the consequences from taxonomy. In contrast, the evolutionary trees from the mature protein-coding region sequences of cDNAs and from the amino acid sequences showed random patterns. These observations indicated that the mature protein-coding region has evolved through a process differently from the untranslated and signal peptide regions. The trees built from the nucleotide differences at each of three positions of codons in the mature protein-coding region suggested that snake-venom-gland PLA2 genes have evolved via a process different from mammalian PLA2 genes. The occurrence of accelerated evolution has been recently discovered in Trimeresurus flavoviridis venom-gland group II PLA2 isozyme genes (Nakashima et al. 1993, Proc Natl Acad Sci USA 90:5964-5968), so the present phylogenetic analysis together with the estimation of nucleotide divergence of cDNAs provides further evidence that snake-venom-group II PLA2 isozyme genes have evolved by accelerated evolution to gain diverse physiological activities.


πŸ“œ SIMILAR VOLUMES


The molecular mechanism of human group I
✍ Maria Chiara Monti; Maria Giovanna Chini; Luigi Margarucci; Alessandra Tosco; Ra πŸ“‚ Article πŸ“… 2009 πŸ› John Wiley and Sons 🌐 English βš– 407 KB

## Abstract The molecular basis of the human group IIA secretory phospholipase A~2~ inactivation by bolinaquinone (BLQ), a hydroxyquinone marine terpenoid, has been investigated for the comprehension of its relevant antiinflammatory properties, through the combination of spectroscopic techniques, b