Trimeresurus flavoviridis venom gland phospholipase A2 isozymes genes have evolved via accelerated substitutions.

T. Ogawa, K. Nakashima, N. Oda, Y. Shimohigashi, M. Ohno, S. Hattori, Masahira Hattori, Y. Sakaki, H. Kihara

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

As a step towards understanding the structure and function of phospholipases A2 (PLA2s), five cDNAs encoding Trimeresurus flavoviridis venom gland PLA2 isozymes have been sequenced. They revealed that the 5' and 3' untranslated regions are much more homologous than the protein-coding regions and that base substitutions have occurred at similar rates for the three positions of codons in the protein-coding regions. Such novel findings are of great interest from the viewpoint of molecular evolution. To gain a further insight into this evolutional phenomenon, we have isolated and sequenced six T. flavoviridis PLA2 isozyme genes. Each gene consisted of four exons and three introns and encoded protein of 138 amino-acid residues, including the signal sequence of 16 amino-acid residues. The introns were much more homologous than the protein-coding regions of exons except for the signal peptide-coding region of the first exon. The absence of apparent functional role in the introns suggested that the protein-coding regions, except for the signal peptide-coding domains, have evolved at greater substitution rates than introns. The fact that the numbers of nucleotide substitutions per non-synonymous site are close to or larger than the numbers of nucleotide substitutions per synonymous site for relevant pairs of genes revealed that Darwinian-type accelerated substitutions have occurred in the protein-coding regions of exons. This is compatible with the presence of PLA2 species with diverse physiological activities in the venom.

Original languageEnglish
Pages (from-to)40-46
Number of pages7
JournalJournal of molecular recognition : JMR
Volume8
Issue number1-2
Publication statusPublished - 1995 Jan
Externally publishedYes

Fingerprint

Phospholipases A2
Venoms
Open Reading Frames
Isoenzymes
Substitution reactions
Genes
Exons
Proteins
Protein Sorting Signals
Introns
Nucleotides
Inteins
Amino acids
Amino Acids
Molecular Evolution
5' Untranslated Regions
3' Untranslated Regions
Codon
Complementary DNA
Trimeresurus venoms

ASJC Scopus subject areas

  • Biochemistry
  • Genetics
  • Molecular Biology
  • Computer Vision and Pattern Recognition
  • Immunology

Cite this

Ogawa, T., Nakashima, K., Oda, N., Shimohigashi, Y., Ohno, M., Hattori, S., ... Kihara, H. (1995). Trimeresurus flavoviridis venom gland phospholipase A2 isozymes genes have evolved via accelerated substitutions. Journal of molecular recognition : JMR, 8(1-2), 40-46.

Trimeresurus flavoviridis venom gland phospholipase A2 isozymes genes have evolved via accelerated substitutions. / Ogawa, T.; Nakashima, K.; Oda, N.; Shimohigashi, Y.; Ohno, M.; Hattori, S.; Hattori, Masahira; Sakaki, Y.; Kihara, H.

In: Journal of molecular recognition : JMR, Vol. 8, No. 1-2, 01.1995, p. 40-46.

Research output: Contribution to journalArticle

Ogawa, T, Nakashima, K, Oda, N, Shimohigashi, Y, Ohno, M, Hattori, S, Hattori, M, Sakaki, Y & Kihara, H 1995, 'Trimeresurus flavoviridis venom gland phospholipase A2 isozymes genes have evolved via accelerated substitutions.', Journal of molecular recognition : JMR, vol. 8, no. 1-2, pp. 40-46.
Ogawa, T. ; Nakashima, K. ; Oda, N. ; Shimohigashi, Y. ; Ohno, M. ; Hattori, S. ; Hattori, Masahira ; Sakaki, Y. ; Kihara, H. / Trimeresurus flavoviridis venom gland phospholipase A2 isozymes genes have evolved via accelerated substitutions. In: Journal of molecular recognition : JMR. 1995 ; Vol. 8, No. 1-2. pp. 40-46.
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