Molecular cloning of horse Hsp90 cDNA and its comparative analysis with other vertebrate Hsp90 sequences.
Molecular cloning of horse Hsp90 cDNA and its comparative analysis with other vertebrate Hsp90 sequences.
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马 Hsp90 cDNA 的分子克隆及其与其他脊椎动物 Hsp90 序列的比较分析。
DOI：
10.1292/jvms.63.115
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发表时间：
2001
期刊：
影响因子：
--
通讯作者：
Kyosuke Nagata
中科院分区：
文献类型：
--
作者：
Kim M. Pepin;F. Momose;Nobushige Ishida;Kyosuke Nagata
热休克蛋白90（Heat shock protein 90，Hsp90）是一种广泛存在的分子伴侣，参与多种细胞过程。为了对基因数据库中相对较少的脊椎动物Hsp90序列做出贡献，我们克隆并测序了马（Equus caballus）Hsp90 α和β cDNA。这使得马的特异性引物的鉴定开发一个方便的PCR为基础的方法，可以监测马的胁迫耐受性。我们将序列数据与其他Hsp90 cDNA序列进行了比较和遗传学分析，并确定了脊椎动物特异性和亚型特异性保守区，以便于将来对Hsp90功能的分子研究。我们发现脊椎动物Hsp90的4个高度保守区域和27个氨基酸在Hsp90 α和Hsp90 β序列之间保守但不同。基于蛋白质的系统发育树揭示了Hsp90 α和β簇内哺乳动物物种之间的高度保守性。核苷酸和氨基酸取代水平的比较表明，马Hsp90 β已经经历了强大的纯化选择，而大鼠Hsp90 β和仓鼠Hsp90 α已被积极选择。令人惊讶的是，鱼类Hsp90 α基因与Hsp90 β基因明显聚在一起，并且没有发现鱼类Hsp90 α蛋白的明显位置。我们的研究结果强调了生物体和亚型特异性Hsp90功能分析在描述Hsp90在细胞中的作用的重要性。
Heat shock protein 90 (Hsp90), a molecular chaperone, is ubiquitous and involved in numerous cellular processes. To contribute to the relatively small collection of vertebrate Hsp90 sequences in the gene data bank, we cloned and sequenced horse (Equus caballus) Hsp90 alpha and beta cDNAs. This enabled identification of horse-specific primers for development of a convenient PCR-based method that could monitor horse stress tolerance. We analyzed the sequence data comparatively and phylogenetically with other Hsp90 cDNA sequences, and identified vertebrate-specific and isoform-specific conserved regions to facilitate future molecular investigations of Hsp90 functions. We found 4 highly conserved regions to vertebrate Hsp90 exclusively and 27 amino acids conserved among but differing between Hsp90 alpha and Hsp90 beta sequences. Protein-based phylogenetic trees revealed high conservation between mammal species within Hsp90 alpha and beta clusters. Comparison of nucleotide and amino acid substitution levels suggests that horse Hsp90 beta has undergone strong purifying selection, while rat Hsp90 beta and hamster Hsp90 alpha have been positively selected. Surprisingly, fish Hsp90 alpha genes clearly clustered with Hsp90 beta genes, and no distinct placement of fish Hsp90 alpha protein was found. The Hsp90 alpha isoform is apparently the result of beta gene duplication. Our results highlight the importance of organism- and isoform-specific Hsp90 functional analyses in describing the role of Hsp90 in cells.
DOI：
10.1016/s0021-9258(18)41621-3
发表时间：
1992-11
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
R. Morimoto;K. Sarge;Klara Abravaya
通讯作者：
R. Morimoto;K. Sarge;Klara Abravaya
90 kDa 热休克蛋白 (hsp-90) 具有 ATP 结合位点和自磷酸化活性。
DOI：
--
发表时间：
1991
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Csermely,P;Kahn,CR
通讯作者：
Kahn,CR