title: Trimeresurus flavoviridis venom gland phospholipase A2 isozymes genes have evolved via accelerated substitutions.
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.
authors.affiliation: Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Ogawa
authors.forename: K
authors.initials: K
authors.lastname: Nakashima
authors.forename: N
authors.initials: N
authors.lastname: Oda
authors.forename: Y
authors.initials: Y
authors.lastname: Shimohigashi
authors.forename: M
authors.initials: M
authors.lastname: Ohno
authors.forename: S
authors.initials: S
authors.lastname: Hattori
authors.forename: M
authors.initials: M
authors.lastname: Hattori
authors.forename: Y
authors.initials: Y
authors.lastname: Sakaki
authors.forename: H
authors.initials: H
authors.lastname: Kihara
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D005075:Biological Evolution; D003001:Cloning, Molecular; D003435:Crotalid Venoms / Q000494:pharmacology / Q000633:toxicity; D017839:Crotalus / Q000235:genetics*; D015698:Genomic Library; D066298:In Vitro Techniques; D007438:Introns; D007527:Isoenzymes / Q000235:genetics* / Q000494:pharmacology / Q000633:toxicity; D008564:Membrane Potentials / Q000187:drug effects; D051379:Mice; D008969:Molecular Sequence Data; D018482:Muscle, Skeletal / Q000187:drug effects / Q000502:physiology; D015345:Oligonucleotide Probes; D010741:Phospholipases A / Q000235:genetics* / Q000494:pharmacology / Q000633:toxicity; D054467:Phospholipases A2; D011892:Rana catesbeiana; D011994:Recombinant Proteins / Q000494:pharmacology / Q000633:toxicity; D012091:Repetitive Sequences, Nucleic Acid; D015183:Restriction Mapping; D017386:Sequence Homology, Amino Acid; D012689:Sequence Homology, Nucleic Acid
chemical_list: D003435:Crotalid Venoms; D007527:Isoenzymes; D015345:Oligonucleotide Probes; D011994:Recombinant Proteins; C029748:Trimeresurus venoms; D010741:Phospholipases A; D054467:Phospholipases A2