嗜热菌HB27的蛋白酪氨酸磷酸酶的折叠研究
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摘要
本研究从嗜热菌T. thermophilus HB27中克隆了一个新的PTPase基因,并在大肠杆菌中成功地表达了可溶的、具有生物学活性的PTPase;建立了简单可行的纯化流程,获得了这个热稳定的蛋白,并对其生物化学性质和去折叠过程进行了详细的研究。具体实验内容及结论如下：
1.利用生物信息学方法,预测PTPase的等电点为5.88,分子量为22.26kDa,其氨基酸出现频率与Swiss-Prot蛋白质序列数据库中的结果存在一定差异,其中极性氨基酸占了55.8%；预测其疏水性最大值为2.433,最小值为-2.222,其中2-18,82-90和140-145位的氨基酸具有一定的疏水性；氨基酸序列同源性分析发现PTPase与来源于T. thermophilus HB8的Tt1001氨基酸序列100%相似,与大鼠PTPase (AAB23588)的氨基酸序列则只有30.5%的相似性；二级结构预测PTPase存在三种二级结构：α螺旋、β折叠和无规卷曲。进化树分析表明该蛋白在进化过程中分支为两类：微生物PTPase与动植物PTPase.
2.以pNPP为底物,研究了不同的pH、温度和离子对PTPase活性的影响,结果显示其最适pH范围为3.6-4.0,最适温度为75℃。30℃和75℃时kcat／Km的值分别为1.77*104M-1·s-1和6.68*105M-1·s-1。Mn2+、Mg2+、Ca2+、Ba2+和Ni2+对PTPase的活性都有激活作用,其激活能力依次下降；而Zn2+,Cu2+,Cl-和SO42-则表现出抑制效应。结果表明PTPase也许在帮助T. thermophilus HB27适应极端温度和特定的生存环境方面在体内发挥着重要的生理作用。
3.脲、盐酸胍和SDS诱导PTPase失活都是可逆的单相反应过程,抑制效应与浓度和时间相关,其IC50值分别为2.65 M、0.24 M和11.27μM；它们均为混合型抑制,在二次作图中前两者表现为直线,而后者为抛物线型。光谱学结果表明脲诱导了PTPase协同性的两态去折叠转变,而低浓度的盐酸胍诱导并稳定了蛋白去折叠中间态；低浓度的SDS诱导了其三级结构的变化和α-螺旋结构的增加,高浓度的SDS稳定了PTPase的二级结构。
4.Cu2+和Zn2+均显著地抑制了PTPase的活性,这种抑制与离子浓度和作用时间相关,其IC50值分别为15μM和8.34 mM；动力学研究表明它们均为混合型可逆抑制,失活过程是单相反应过程。光谱学结果表明它们诱导了PTPase的三级结构发生了变化,但并不影响其二级结构。EDTA无法使Cu2+失活的PTPase恢复活性,但添加DTT则能使其活性恢复到其天然态时的40%,推测PTPase活性位点的Cys残基很可能被Cu2+氧化,从而导致其活性丧失和三级结构发生变化。
综上,本研究为理解这一新的热稳定性PTPase的耐热机制、折叠机理、结构和功能,并为构建高效耐热的工程菌及其工业化应用提供了一些有用的信息,同时,对以PTPase为药物作用靶标研发其抑制剂类药物,以期治疗与PTPase相关的人类疾病也有一定的参考意义。
In this research, we have cloned the full-length sequence encoding PTPase gene from the genomic DNA of T. thermophilus HB27 and expressed the active and soluble recombinant PTPase successfully in E. coli. After a simple purification procedure, we obtained this thermostable enzyme, and then characterized its biochemical and unfolding properties in detail in the following study. Our findings are stated below:
1. With the aids of bioinformatics, the pI and molecular weight were estimated to be 5.88 and 22.26 kDa, respectively. There were some differences in amino acid frequences between PTPase of T. thermophilus HB27 and Swiss-Port protein sequence database. The content of polar amino acids was 55.8%. The maximum and minimum of hydrophobicity were 2.433 and-2.222, respectively. The amino acid sequences at the positions of 2～18,82-90 and 140-145 were hydrophobic. The sequence alignment indicated that there was 100% similarity in amino acid sequences between PTPase of T. thermophilus HB27 and Tt1001 of T. thermophilus HB8, but had only 30.5% similarity with PTPase (AAB23588) of rats liver. Three types of secondary structuresα-helix,β-sheet and random coil) existed in PTPase according to the secondary structure prediction. Phylogenetic tree analysis showed that PTPase were evolved into two types of branches in the process of evolution:microbial PTPase and PTPase of plants and animals.
2. The effects of pH, temperature and ions on the activity of PTPase were studied when using pNPP as the substrate. The results showed a optimum pH range of 3.6～4.0 and optimum temperature of 75℃. k_(cat)/K_m were 1.77*10~4 M~(-1) and 6.68*10~5 M~(-1)·s~(-1)at 30℃and 75℃, respectively. Its activity could be activated by Mn~(2+), followed by the order of Mg~(2+), Ca~(2+), Ba~(2+)and Ni~(2+), but inhibited by Zn~(2+), Cu~(2+), Cl" and SO_4~(2-). These results suggested that PTPase might play important physiological roles in vivo to adapt T. thermophilus HB27 to the extreme temperatures and specific nutritional conditions.
3. The activity and conformational changes of PTPase were investigated in the presence of urea, GdnHCl and SDS. The results showed the activity of PTPase was inactivated by these denaturants in a concentration and time-dependent manner. The IC_(50) value were 2.65 M,0.24 M and 11.27μM, respectively. Inactivation kinetics revealed that all of them were reversible mixed-type inhibition and the inactivation was mono-phase process. Urea and GdnHCl denaturation were showed to be a line in the secondary plot, while SDS was a parabola. Spectral analysis indicated that the unfolding of PTPase induced by urea was a two-state transition whereas in the case of GdnHCl, intermediate was induced and stabilized at lower concentrations. At lower concentration, SDS induced the changes of the tertiary structures and the increase of a-helix structures of PTPase. The high content of secondary structure was stabilized by higher concentration SDS.
4. The activity of PTPase was significantly inhibited by Cu~(2+)and Zn~(2+)in a concentration-and time-dependent manner. TheiC_(50) value were 15μM and 8.34 mM, respectively. Sequential kinetic studies suggested that both of them induced a reversible mixed-type inhibition and the inactivation was a mono-phase process. The spectral studies showed that both of them induced the tertiary conformational changes of PTPase, but did not change its secondary structures. The PTPase inactivated by Cu~(2+)could not be reactivated by EDTA, but reactivated up to 40%of native activity with DTT treatment. Probably, the cysteine residues located around the active sites of PTPase were oxidized by Cu~(2+), which further resulted in the inactivation and the tertiary conformational changes of PTPase.
In conclusion, this study is useful to understand its heat-resistant mechanism, folding mechanism, structure and function of this new thermostable PTPase, as well as the construct of high efficient and heat-tolerant engineering strains and their possible applications in industry. In addition, it is meaningful to develop the drugs with PTPase as the targets in order to treat human diseases with relation to PTPase with the inhibitors of PTPase.
1.利用生物信息学方法,预测PTPase的等电点为5.88,分子量为22.26kDa,其氨基酸出现频率与Swiss-Prot蛋白质序列数据库中的结果存在一定差异,其中极性氨基酸占了55.8%；预测其疏水性最大值为2.433,最小值为-2.222,其中2-18,82-90和140-145位的氨基酸具有一定的疏水性；氨基酸序列同源性分析发现PTPase与来源于T. thermophilus HB8的Tt1001氨基酸序列100%相似,与大鼠PTPase (AAB23588)的氨基酸序列则只有30.5%的相似性；二级结构预测PTPase存在三种二级结构：α螺旋、β折叠和无规卷曲。进化树分析表明该蛋白在进化过程中分支为两类：微生物PTPase与动植物PTPase.
2.以pNPP为底物,研究了不同的pH、温度和离子对PTPase活性的影响,结果显示其最适pH范围为3.6-4.0,最适温度为75℃。30℃和75℃时kcat／Km的值分别为1.77*104M-1·s-1和6.68*105M-1·s-1。Mn2+、Mg2+、Ca2+、Ba2+和Ni2+对PTPase的活性都有激活作用,其激活能力依次下降；而Zn2+,Cu2+,Cl-和SO42-则表现出抑制效应。结果表明PTPase也许在帮助T. thermophilus HB27适应极端温度和特定的生存环境方面在体内发挥着重要的生理作用。
3.脲、盐酸胍和SDS诱导PTPase失活都是可逆的单相反应过程,抑制效应与浓度和时间相关,其IC50值分别为2.65 M、0.24 M和11.27μM；它们均为混合型抑制,在二次作图中前两者表现为直线,而后者为抛物线型。光谱学结果表明脲诱导了PTPase协同性的两态去折叠转变,而低浓度的盐酸胍诱导并稳定了蛋白去折叠中间态；低浓度的SDS诱导了其三级结构的变化和α-螺旋结构的增加,高浓度的SDS稳定了PTPase的二级结构。
4.Cu2+和Zn2+均显著地抑制了PTPase的活性,这种抑制与离子浓度和作用时间相关,其IC50值分别为15μM和8.34 mM；动力学研究表明它们均为混合型可逆抑制,失活过程是单相反应过程。光谱学结果表明它们诱导了PTPase的三级结构发生了变化,但并不影响其二级结构。EDTA无法使Cu2+失活的PTPase恢复活性,但添加DTT则能使其活性恢复到其天然态时的40%,推测PTPase活性位点的Cys残基很可能被Cu2+氧化,从而导致其活性丧失和三级结构发生变化。
综上,本研究为理解这一新的热稳定性PTPase的耐热机制、折叠机理、结构和功能,并为构建高效耐热的工程菌及其工业化应用提供了一些有用的信息,同时,对以PTPase为药物作用靶标研发其抑制剂类药物,以期治疗与PTPase相关的人类疾病也有一定的参考意义。
In this research, we have cloned the full-length sequence encoding PTPase gene from the genomic DNA of T. thermophilus HB27 and expressed the active and soluble recombinant PTPase successfully in E. coli. After a simple purification procedure, we obtained this thermostable enzyme, and then characterized its biochemical and unfolding properties in detail in the following study. Our findings are stated below:
1. With the aids of bioinformatics, the pI and molecular weight were estimated to be 5.88 and 22.26 kDa, respectively. There were some differences in amino acid frequences between PTPase of T. thermophilus HB27 and Swiss-Port protein sequence database. The content of polar amino acids was 55.8%. The maximum and minimum of hydrophobicity were 2.433 and-2.222, respectively. The amino acid sequences at the positions of 2～18,82-90 and 140-145 were hydrophobic. The sequence alignment indicated that there was 100% similarity in amino acid sequences between PTPase of T. thermophilus HB27 and Tt1001 of T. thermophilus HB8, but had only 30.5% similarity with PTPase (AAB23588) of rats liver. Three types of secondary structuresα-helix,β-sheet and random coil) existed in PTPase according to the secondary structure prediction. Phylogenetic tree analysis showed that PTPase were evolved into two types of branches in the process of evolution:microbial PTPase and PTPase of plants and animals.
2. The effects of pH, temperature and ions on the activity of PTPase were studied when using pNPP as the substrate. The results showed a optimum pH range of 3.6～4.0 and optimum temperature of 75℃. k_(cat)/K_m were 1.77*10~4 M~(-1) and 6.68*10~5 M~(-1)·s~(-1)at 30℃and 75℃, respectively. Its activity could be activated by Mn~(2+), followed by the order of Mg~(2+), Ca~(2+), Ba~(2+)and Ni~(2+), but inhibited by Zn~(2+), Cu~(2+), Cl" and SO_4~(2-). These results suggested that PTPase might play important physiological roles in vivo to adapt T. thermophilus HB27 to the extreme temperatures and specific nutritional conditions.
3. The activity and conformational changes of PTPase were investigated in the presence of urea, GdnHCl and SDS. The results showed the activity of PTPase was inactivated by these denaturants in a concentration and time-dependent manner. The IC_(50) value were 2.65 M,0.24 M and 11.27μM, respectively. Inactivation kinetics revealed that all of them were reversible mixed-type inhibition and the inactivation was mono-phase process. Urea and GdnHCl denaturation were showed to be a line in the secondary plot, while SDS was a parabola. Spectral analysis indicated that the unfolding of PTPase induced by urea was a two-state transition whereas in the case of GdnHCl, intermediate was induced and stabilized at lower concentrations. At lower concentration, SDS induced the changes of the tertiary structures and the increase of a-helix structures of PTPase. The high content of secondary structure was stabilized by higher concentration SDS.
4. The activity of PTPase was significantly inhibited by Cu~(2+)and Zn~(2+)in a concentration-and time-dependent manner. TheiC_(50) value were 15μM and 8.34 mM, respectively. Sequential kinetic studies suggested that both of them induced a reversible mixed-type inhibition and the inactivation was a mono-phase process. The spectral studies showed that both of them induced the tertiary conformational changes of PTPase, but did not change its secondary structures. The PTPase inactivated by Cu~(2+)could not be reactivated by EDTA, but reactivated up to 40%of native activity with DTT treatment. Probably, the cysteine residues located around the active sites of PTPase were oxidized by Cu~(2+), which further resulted in the inactivation and the tertiary conformational changes of PTPase.
In conclusion, this study is useful to understand its heat-resistant mechanism, folding mechanism, structure and function of this new thermostable PTPase, as well as the construct of high efficient and heat-tolerant engineering strains and their possible applications in industry. In addition, it is meaningful to develop the drugs with PTPase as the targets in order to treat human diseases with relation to PTPase with the inhibitors of PTPase.
引文
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