First report of a peroxiredoxin homologue in jellyfish: molecular cloning, expression and functional characterization of CcPrx4 from Cyanea capillata.
First report of a peroxiredoxin homologue in jellyfish: molecular cloning, expression and functional characterization of CcPrx4 from Cyanea capillata.
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水母中过氧化还原蛋白同源物的首次报告：来自 Cyanea capillata 的 CcPrx4 的分子克隆、表达和功能表征
DOI：
10.3390/md12010214
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发表时间：
2014-01-09
期刊：
影响因子：
5.4
通讯作者：
Zhang L
中科院分区：
文献类型：
--
作者：
Ruan Z;Liu G;Wang B;Zhou Y;Lu J;Wang Q;Zhao J;Zhang L
我们首次从毛囊水母触须的cDNA文库中鉴定并鉴定了一种新的过氧化还蛋白，命名为CcPrx4。CcPrx4基因全长由884个核苷酸组成，编码247个氨基酸的成熟蛋白。它与过氧化还蛋白4(Prx4)具有高度保守的F基序(93FTFVCPTEI101)、疏水区(217VCPAGW222)、140GGLG143和239YF240的同源性，表明它应该是Prx4家族的一个新成员。推导的CcPrx4蛋白的计算相对分子质量为27.2 kDa，等电点估计为6.3。实时荧光定量聚合酶链式反应分析表明，在所分析的所有水母组织中均可检测到CcPrx4基因的表达。将CcPrx4蛋白克隆到表达载体pET-24a中，在大肠杆菌Rosetta(DE3)pLysS中表达。用HisTrap高效螯合柱层析纯化重组CcPrx4蛋白，并对其生物学功能进行分析。结果表明，纯化的重组CcPrx4蛋白具有还原过氧化氢和保护超螺旋DNA免受氧化损伤的能力，提示CcPrx4蛋白可能在保护水母免受氧化损伤中发挥重要作用。
We first identified and characterized a novel peroxiredoxin (Prx), designated as CcPrx4, from the cDNA library of the tentacle of the jellyfish Cyanea capillata. The full-length cDNA sequence of CcPrx4 consisted of 884 nucleotides with an open reading frame encoding a mature protein of 247 amino acids. It showed a significant homology to peroxiredoxin 4 (Prx4) with the highly conserved F-motif (93FTFVCPTEI101), hydrophobic region (217VCPAGW222), 140GGLG143 and 239YF240, indicating that it should be a new member of the Prx4 family. The deduced CcPrx4 protein had a calculated molecular mass of 27.2 kDa and an estimated isoelectric point of 6.3. Quantitative real-time PCR analysis showed that CcPrx4 mRNA could be detected in all the jellyfish tissues analyzed. CcPrx4 protein was cloned into the expression vector, pET-24a, and expressed in Escherichia coli Rosetta (DE3) pLysS. Recombinant CcPrx4 protein was purified by HisTrap High Performance chelating column chromatography and analyzed for its biological function. The results showed that the purified recombinant CcPrx4 protein manifested the ability to reduce hydrogen peroxide and protect supercoiled DNA from oxidative damage, suggesting that CcPrx4 protein may play an important role in protecting jellyfish from oxidative damage.
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影响因子：
3.8
作者：
Lee, KS;Kim, SR;Jin, BR
通讯作者：
Jin, BR
DOI：
10.1016/j.bbrc.2007.11.114
发表时间：
2008-02-08
影响因子：
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作者：
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作者：
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影响因子：
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作者：
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通讯作者：
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