Molecular cloning of a cDNA encoding a Xenopus laevis 70-kDa heat shock cognate protein, hsc70.II

被引:13
作者
Ali, A
SalterCid, L
Flajnik, MJ
Heikkila, JJ
机构
[1] UNIV WATERLOO,DEPT BIOL,WATERLOO,ON N2L 3G1,CANADA
[2] UNIV MIAMI,DEPT MICROBIOL & IMMUNOL,MIAMI,FL 33101
来源
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION | 1996年 / 1309卷 / 03期
关键词
heat shock protein; heat shock cognate; chaperone; Hsc70; (Xenopus);
D O I
10.1016/S0167-4781(96)00156-X
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
We have isolated and sequenced a full-length cDNA clone encoding a Xenopus laevis 70 kDa heat shock cognate protein, hsc70.II. The protein coding region exhibited high identity with Xenopus hsc70.I (94%), suggesting that the two genes are the result of a genomic tetraploidization event which occurred in Xenopus over 30 million years ago. Also, hsc70.II displayed a high level of identity with mammalian hsc70. However, the identity of Xenopus hsc70.II cDNA with Xenopus hsp70 was only 82%. At the carboxyl end of the hsc70.II protein, the identity with hsc70.I was 85%, while the identity for hsp70 was only 58%, These data support the theory that the inducible and constitutive members of the hsp70 family diverged well before the emergence of amphibians. Also, hsc70.II contains a number of conserved elements including an ATP-binding domain, a nuclear localization signal and the carboxyl terminal motif, EEVD, which may have a role in chaperone function.
引用
收藏
页码:174 / 178
页数:5
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