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Regional and accelerated molecular evolution in group I snake venom gland phospholipase A2 isozymes.
Chuman, Y; Nobuhisa, I; Ogawa, T; Deshimaru, M; Chijiwa, T; Tan, N H; Fukumaki, Y; Shimohigashi, Y; Ducancel, F; Boulain, J C; Ménez, A; Ohno, M.
Afiliação
  • Chuman Y; Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka, Japan.
Toxicon ; 38(3): 449-62, 2000 Mar.
Article em En | MEDLINE | ID: mdl-10669032
ABSTRACT
In accordance with detection of a few phospholipase A2 (PLA2) isozyme genes by Southern blot analysis, only two cDNAs, named NnkPLA-I , and NnkPLA-II, encoding group I PLA2s, NnkPLA-I and NnkPLA-II, respectively, were isolated from the venom gland cDNA library of Elapinae Naja naja kaouthia of Malaysia. NnkPLA-I and NnkPLA-II showed four amino acid substitutions, all of which were brought about by single nucleotide substitution. No existence of clones encoding CM-II and CM-III, PLA2 isozymes which had been isolated from the venom of N. naja kaouthia of Thailand, in Malaysian N. naja kaouthia venom gland cDNA library was verified by dot blot hybridization analysis with particular probes. NnkPLA-I and NnkPLA-II differed from CM-II and CM-III with four and two amino acid substitutions, respectively, suggesting that their molecular evolution is regional. The comparison of NnkPLA-I, NnkPLA-II and cDNAs encoding other group I snake venom gland PLA2s indicated that the 5'- and 3'-untranslated regions are more conserved than the mature protein-coding region and that the number of nucleotide substitutions per nonsynonymous site is almost equal to that per synonymous site in the protein-coding region, suggesting that accelerated evolution has occurred in group I venom gland PLA2s possibly to acquire new physiological functions.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fosfolipases A / Venenos de Serpentes / Evolução Molecular / Glândulas Exócrinas Idioma: En Revista: Toxicon Ano de publicação: 2000 Tipo de documento: Article País de afiliação: Japão
Buscar no Google
Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fosfolipases A / Venenos de Serpentes / Evolução Molecular / Glândulas Exócrinas Idioma: En Revista: Toxicon Ano de publicação: 2000 Tipo de documento: Article País de afiliação: Japão