title: Molecular evolution of toxin genes in Elapidae snakes.
abstract: The venom of the sea krait, Laticauda semifasciata, consists primarily of two toxic proteins, phospholipase A(2) (PLA(2)) and a three-finger-structure toxin. We have cloned both toxic protein genes, including the upstream region. PLA(2) genes contain three types of inserted sequences: an AG-rich region, a chicken repeat 1-like long interspersed nucleotide element sequence and an intron II 3' side repeat sequence. The molecular divergence of L. semifasciata PLA(2) genes was defined on the basis of the inserted sequences and their sequence homology. The length of intron I in the three-finger-structure toxin genes differs from species to species. The alignment analysis of intron I of the three-finger-structure toxin genes revealed that the intron I sequence of the ancestral gene comprised ten genetic regions. A hypothetical evolutionary process for the three-finger-structure toxin genes has also been developed.
authors.affiliation: Department of Chemistry, Faculty of Science and Technology, Sophia University, Tokyo, Japan. t_tamiya@sophia.ac.jp
authors.forename: Toru
authors.initials: T
authors.lastname: Tamiya
authors.forename: Takahiko J
authors.initials: TJ
authors.lastname: Fujimi
mesh_terms: D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D017815:Elapidae / Q000235:genetics*; D019143:Evolution, Molecular; D005796:Genes; D008969:Molecular Sequence Data; D010741:Phospholipases A / Q000235:genetics*; D030162:Reptilian Proteins / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid; D014118:Toxins, Biological / Q000235:genetics*
chemical_list: D030162:Reptilian Proteins; D014118:Toxins, Biological; D010741:Phospholipases A