Characterization of mitochondria-located small heat shock protein from tomato (Lycopersicon esculentum)
Characterization of mitochondria-located small heat shock protein from tomato (Lycopersicon esculentum)
复制标题
DOI：
10.1093/oxfordjournals.pcp.a029518
复制
发表时间：
1999-12-01
影响因子：
4.9
通讯作者：
Shono, M
中科院分区：
文献类型：
--
作者：
Liu, JA;Shono, M
我们克隆并测序了番茄小心脏休克蛋白（MT-sHSP）基因前体（LeHSP 23.8）的全长cDNA。推导的蛋白质前体与计算的分子量为23.8 kDa的预测为目标线粒体，并被归类为植物MT-sHSP。Southern印迹分析表明，番茄基因组DNA中存在一个LeHSP 23.8的单拷贝。Northern-blot分析显示LeHSP 23.8 mRNA具有热诱导特性。LeHSP 23.8 mRNA在36 ℃左右几乎检测不到，但在40 ℃时显著积累。LeHSP 23.8的分子伴侣功能在体外得到证实。重组LeHSP 23.8能够增强化学变性的柠檬酸合酶（CS）的复性。此外，重组LeHSP 23.8保护CS从热失活，也促进热失活的柠檬酸合酶的复性。
We cloned and sequenced a full-length cDNA encoding the precursor of the mitochondria-located small heart shock protein (MT-sHSP) gene (LeHSP23.8) from tomato (Lycopersicon esculentum). The deduced protein precursor with a calculated molecular weight of 23.8 kDa was predicted to target mitochondria and was classified as a plant MT-sHSP. A single copy of LeHSP23.8 was found in tomato genomic DNA by southern-blot analysis. Northern-blot analysis revealed the heat inducible character of LeHSP23.8 mRNA. The LeHSP23.8 mRNA was hardly detectable at about 36 degrees C but accumulated markedly at 40 degrees C. The molecular chaperone function of LeHSP23.8 was confirmed in vitro. The recombinant LeHSP23.8 was able to enhance the renaturation of chemically denatured citrate synthase (CS). Moreover, the recombinant LeHSP23.8 protected CS from thermal inactivation and also promoted the renaturation of thermally inactivated citrate synthase.