cDNA cloning of turtle prion protein

被引：81

作者：

Simonic, T ^{[1
]}

Duga, S ^{[1
]}

Strumbo, B ^{[1
]}

Asselta, R ^{[1
]}

Ceciliani, F ^{[1
]}

Ronchi, S ^{[1
]}

机构：

[1] Univ Milan, Ist Fisiol Vet & Biochim, I-20133 Milan, Italy

来源：

FEBS LETTERS | 2000年 / 469卷 / 01期

关键词：

reptile prion protein; cDNA cloning; gene organization; EF-hand Ca2+ binding motif;

D O I：

10.1016/S0014-5793(00)01232-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Cloning of the cDNA coding for the 270-residue turtle prion protein is reported. It represents the most remote example thus far described. The entire coding region is comprised in a single exon, while a large intron interrupts the 5' UTR. The common structural features of the known prion proteins are all conserved in turtle PrP, whose identity degree to mammalian and avian proteins is about 40 and 58%, respectively. The most intriguing feature, unique to the turtle prion, is the presence of an EF-hand Ca2+ binding motif in the C-terminal half of the protein. (C) 2000 Federation of European Biochemical Societies.

引用

页码：33 / 38

页数：6

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