HspB3, the most deviating of the six known human small heat shock proteins

被引:48
作者
Boelens, WC [1 ]
Van Boekel, MAM [1 ]
De Jong, WW [1 ]
机构
[1] Univ Nijmegen, Dept Biochem, NL-6500 HB Nijmegen, Netherlands
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1998年 / 1388卷 / 02期
关键词
small heat shock protein; sHsp; alpha-crystallin;
D O I
10.1016/S0167-4838(98)00215-5
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
From the alignment of 14 EST clones, the cDNA sequence of a novel human small heat shock protein (sHsp), called HspB3, could be deduced. The 3' part of the HspB3 cDNA is 99% identical to that of the previously reported HspL27 cDNA (W.Y. Lam, S.K. Wing Tsui, P.T. Law, S.C. Luk, K.P. Fung, C.Y. Lee, M.M. Waye, Isolation and characterization of a human heart cDNA encoding a new member of the small heat shock protein family-HSPL27, Biochim. Biophys. Acta 1314 (1996) 120-124). We argue that the HspB3 cDNA sequence is a corrected version of the HspL27 cDNA. The HspB3 cDNA is 742 bp long and contains an open reading frame specifying a polypeptide of 150 amino acid residues. Among the six known human sHsps it is evident that HspB3 is the most deviating one, having a unique N-terminal domain and essentially lacking a C-terminal extension. Northern blot analysis shows that in smooth muscle tissue the cDNA hybridizes with mRNA of about 0.9 kb. (C) 1998 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:513 / 516
页数:4
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