Accelerated evolution of crotalinae snake venom gland serine proteases

FEBS Letters

Fukumaki, Yasuyuki⁵  Nobuhisa, Ikuo⁴  Ohno, Motonori⁴  Deshimaru, Masanobu⁴  Nakashima, Kin-ichi⁴  Ogawa, Tomohisa⁴  Niwa, Mineo³  Shimohigashi, Yasuyuki⁴  Hattori, Shosaku¹  Yamashina, Ikuo²  Chijiwa, Takahito⁴ 

[1] Institute for Medical Science, University of Tokyo, Oshima-gun, Kagoshima 894-15, Japan;Faculty of Engineering, Kyoto Industrial University, Kita-ku, Kyoto 603, Japan;Faculty of Pharmaceutical Sciences, Tokushima University, Tokushima, Tokushima 770, Japan;Department of Chemistry, Faculty of Science, Kyushu University, Higashi-ku, Fukuoka 812, Japan;Institute of Genetic Information, Kyushu University, Higashi-ku, Fukuoka 812, Japan

关键词: Snake venom;    Serine protease family;    cDNA cloning;    Evolution;    KLE;    kallikrein-like enzyme;    CPI;    capillary permeability increasing;    PLA2;    phospholipase A2;    TBP;    TATA box binding protein;    PCR;    polymerase chain reaction;    RT;    reverse transcription;    UTR;    untranslated region;   

DOI  :  10.1016/S0014-5793(96)01144-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Eight cDNAs encoding serine proteases isolated from Trimeresurus flavoviridis (habu snake) and T. gramineus (green habu snake) venom gland cDNA libraries showed that nonsynonymous nucleotide substitutions have accumulated in the mature protein-coding regions to cause amino acid changes. Southern blot analysis of T. flavoviridis genomic DNAs using two proper probes indicated that venom gland serine protease genes form a multigene family in the genome. These observations suggest that venom gland serine proteases have diversified their amino acid sequences in an accelerating manner. Since a similar feature has been previously discovered in crotalinae snake venom gland phospholipase A₂ (PLA₂) isozyme genes, accelerated evolution appears to be universal in plural isozyme families of crotalinae snake venom gland.

【 授权许可】

Unknown