节杆菌电转化方法的优化及6-磷酸海藻糖酯酶基因的功能研究
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摘要
节杆菌是土壤中最常分离到的土著性需氧微生物。节杆菌属的成员不仅可以降解各种环境污染物,而且有能力抵御各种环境压力,例如低温、干燥、饥饿、电离辐射、高渗透压等。有报道指出,节杆菌的抗逆性可能与其体内存在多种海藻糖合成的基因有关。在大多数生物体内,海藻糖主要生物合成途径包含6-磷酸海藻糖合成酶(TPS)和6-磷酸海藻糖酯酶(TPP)。由于TPP丰富的生物学功能及其在抗逆境胁迫中可能发挥的重要作用引起了人们极大的兴趣。然而目前有关TPP的研究主要集中在高温和中温微生物中,在低温微生物中还未见报道；而且对这些基因进行克隆、过表达、敲除以及合成途径的研究离不开高效的转化系统。因此,本研究采用节杆菌典型的组成型表达载体pART2对一株耐冷菌Arthrobacter sp. A3进行电转化条件的优化研究,并进一步对TPP的功能进行了深入研究。获得的主要研究结果如下：
(1)通过对整个电转化过程中所涉及的因素进行系统分析,首次建立了一种简单、快速、转化水平最高的适用于节杆菌属的高效电转化方法。在所测定的因素中,在细胞对数生长初期加入青霉素处理,以及电击与复苏基质中0.5 M山梨醇的存在,可以导致转化效率增加幅度最大并使结果具有一致性；在最优化的电击条件下,Arthrobacter sp. A3的转化效率可达到6.8×107个转化子/μgpART2;可以保证一个转化实验在10分钟内完成；成功将该方法应用于节杆菌的其他5种典型物种,都得到了较高的转化效率。这一方法是节杆菌基因操作的有效工具,有助于推动这一具有重要经济意义的生物群体的研究。
(2)克隆得到Arthrobacter sp. A3 6-磷酸海藻糖酯酶基因。通过热不对称交错RCR (TAIL-PCR),从Arthrobacter sp. A3中得到编码6-磷酸海藻糖酯酶的基因tpp,该基因含有801bp的开放阅读框,编码266个氨基酸；通过生物信息学分析其氨基酸序列,发现不具有信号肽序列和跨膜区,表明TPP为胞内酶；BLASTP结果显示TPP属于HAD超家族。
(3)实现Arthrobacter sp. A3 tpp基因在大肠杆菌中的异源表达,并完成了重组TPP的纯化。重组酶在表观上与预测的分子量27.9 kDa一致。
(4)阐明了来源于Arthrobacter sp. A3的重组TPP可能是一种新的适冷酶。研究发现该酶表现出对Mg~(2+)或Co~(2+)的绝对需求; Arthrobacter sp. A3 TPP最适pH值范围较宽(5.0～7.5),而其他验证功能的6-磷酸海藻糖酯酶却无此特征；TPP最适反应温度约为30℃,也是重组TPP酶达到最高Kcat/Km(催化效率)时的温度；TPP在4℃可以保持最大活性的75%,表明该酶在低温下稳定；在50℃热激处理6分钟就会失去70%的活性,说明该酶通常不耐热；重组TPP Kcat/Km最大值为37.5mM-1·s-1,远远高于已报道的来源于中温菌大肠杆菌的TPP。在20℃时,重组TPP Km值达到最小,但是,即使在4℃,相比于其他已经报道的微生物的TPP,该酶仍具有最低的Km值。所有这些特性都与适冷酶的特征相吻合。
(5)揭示了tpp在Arthrobacter sp. A3抵御低温胁迫中具有重要作用。实现Arthrobacter sp. A3 tpp基因的同源表达；我们发现在Arthrobacter sp. A3体内过表达tpp,可以使该菌0℃时的生存率略有提高。tpp过表达菌株在0℃生存率的提高,以及TPP较低的最适温度水平和低温下保持高催化效率的特征,表明tpp与Arthrobacter sp. A3在低温下生存具有一定相关性。
综上所述,本研究对来源于耐冷节杆菌属TPP进行了首次报道。不仅为节杆菌tpp功能研究提供了科学依据,而且为研究低温菌蛋白以及节杆菌适应低温环境的作用机制奠定了理论基础。
Strains of Arthrobacter are among the most frequently isolated, indigenous, aerobic bacteria found in soils. Members of the genus are known to biodegrade organic compounds in the environment and have the ability to withstand various environmental stresses, such as cold, desiccation, starvation, ionizing radiation, and osmotic stress. The presence of genes for trehalose synthesis in Arthrobacter might be important for this organism's resistance to environmental stresses. The major pathway for trehalose biosynthesis in most organisms involves two enzymes, trehalose-6-phosphate synthase (TPS) and trehalose-6-phosphate phosphatase (TPP). TPP has received great interest because of its abundant biological functions and potential importance for resistance to environmental stresses. Although TPP has been studied in thermophiles and mesophiles, few of them were characterized in cold-adapted microorganisms. A prerequisite for genetic manipulations of these specific genes in Arthrobacter is a high efficiency transformation system that allows for gene cloning, overexpression, and knock-out, as well as for studying trehalose biosynthetic pathway. Thus, in this study, a constitutive gene expression vector pART2 was selected to optimize the electroporation conditions for Arthrobacter sp. A3. Furthermore, the biochemical properties of TPP were studied in this psychrotrophic bacterium. The main results of the present study are as follows:
(1) A simple, rapid, and highly efficient electroporation method which was suitable for Arthrobacter species was established through a systematic examination of the factors involved in the entire electroporation process. Of the parameters assayed, the addition of penicillin to cells during the early log phase of growth and the presence of 0.5 M sorbitol in the electroporation and recovery media produced the greatest increases in transformation efficiency and consistency of results. Using optimum conditions, we generally achieved an efficiency of 6.8 x 10'transformants per microgram of pART2 for Arthrobacter sp. A3. To our knowledge, this level of electro-competence is the highest ever reported for the Arthrobacter genus. The proposed method allows a transformation trial to be accomplished in 10 minutes. This protocol was also successfully applied to other five Arthrobacter species. This method constitutes a useful tool for the genetic manipulations of Arthrobacter, and will facilitate research of this economically important group of organism.
(2) The tpp gene encoding trehalose-6-phosphate phosphatase from Arthrobacter sp. A3 was obtained by thermal asymmetric interlaced PCR (TAIL-PCR). The gene contained a 801-bp open reading frame encoding 266 amino acids. The result of amino acid sequence analysis by bioinformatics showed that there was no signal peptide and transmembrane domain, which indicated that the TPP of Arthrobacter sp. A3 was an intracellular enzyme. BLASTP result revealed that TPP belonged to the HAD superfamily.
(3) The tpp gene was expressed heterogenously in Escherichia coli, and the recombinant enzyme was purified to apparent homogeneity with a calculated molecular weight of 27.9 kDa.
(4) The properties of recombinant TPP were characterized in detail. This enzyme showed an absolute requirement for Mg~(2+)or Co~(2+). The Arthrobacter sp. A3 TPP showed a broad pH optimum range (from pH 5.0 to 7.5), whereas other trehalose-6-phosphate phosphatase characterised do not possess this feature. The temperature optimum was about 30℃, which was also the point of the highest Kcat/Km value (catalytic efficiency) for the recombinant TPP enzyme. The enzyme was stable at low temperatures, as it could maintain 75%of the maximal activity at 4℃. On the other hand, the enzyme was generally heat-labile, losing 70%of its activity when subjected to heat treatment at 50℃for 6 min. The highest Kcat/Km value was 37.5 mM-1·s-1, which was much higher than values published for mesphilic E.coli TPP. The lowest Km value was at 20℃, however, even at 4℃, it possessed the lowest Km value compared to the counterparts from the other reported microorganisms. These characteristics may suggest that this TPP is a novel cold-adapted enzyme.
(5) The tpp gene was expressed homologously in Arthrobacter sp. A3. Overexpression of tpp in Arthrobacter sp. A3 could increase the cell viability slightly at 0℃. The enhancement of viability of tpp-overproducing strain at 0℃, together with the low optimal temperature and the high-catalytic efficiency of TPP at low temperature may indicate that this TPP plays an important role in resistance of Arthrobacter sp. A3 to cold.
This is the first report of the characterization of TPP from psychrotrophic Arthrobacter genus. The research of this paper would provide more knowledge to the functions of TPP, and provide basic information for cold-adapted enzymes, and also provide foundation for further understanding the survival strategies of Arthrobacter at low temperatures.
(1)通过对整个电转化过程中所涉及的因素进行系统分析,首次建立了一种简单、快速、转化水平最高的适用于节杆菌属的高效电转化方法。在所测定的因素中,在细胞对数生长初期加入青霉素处理,以及电击与复苏基质中0.5 M山梨醇的存在,可以导致转化效率增加幅度最大并使结果具有一致性；在最优化的电击条件下,Arthrobacter sp. A3的转化效率可达到6.8×107个转化子/μgpART2;可以保证一个转化实验在10分钟内完成；成功将该方法应用于节杆菌的其他5种典型物种,都得到了较高的转化效率。这一方法是节杆菌基因操作的有效工具,有助于推动这一具有重要经济意义的生物群体的研究。
(2)克隆得到Arthrobacter sp. A3 6-磷酸海藻糖酯酶基因。通过热不对称交错RCR (TAIL-PCR),从Arthrobacter sp. A3中得到编码6-磷酸海藻糖酯酶的基因tpp,该基因含有801bp的开放阅读框,编码266个氨基酸；通过生物信息学分析其氨基酸序列,发现不具有信号肽序列和跨膜区,表明TPP为胞内酶；BLASTP结果显示TPP属于HAD超家族。
(3)实现Arthrobacter sp. A3 tpp基因在大肠杆菌中的异源表达,并完成了重组TPP的纯化。重组酶在表观上与预测的分子量27.9 kDa一致。
(4)阐明了来源于Arthrobacter sp. A3的重组TPP可能是一种新的适冷酶。研究发现该酶表现出对Mg~(2+)或Co~(2+)的绝对需求; Arthrobacter sp. A3 TPP最适pH值范围较宽(5.0～7.5),而其他验证功能的6-磷酸海藻糖酯酶却无此特征；TPP最适反应温度约为30℃,也是重组TPP酶达到最高Kcat/Km(催化效率)时的温度；TPP在4℃可以保持最大活性的75%,表明该酶在低温下稳定；在50℃热激处理6分钟就会失去70%的活性,说明该酶通常不耐热；重组TPP Kcat/Km最大值为37.5mM-1·s-1,远远高于已报道的来源于中温菌大肠杆菌的TPP。在20℃时,重组TPP Km值达到最小,但是,即使在4℃,相比于其他已经报道的微生物的TPP,该酶仍具有最低的Km值。所有这些特性都与适冷酶的特征相吻合。
(5)揭示了tpp在Arthrobacter sp. A3抵御低温胁迫中具有重要作用。实现Arthrobacter sp. A3 tpp基因的同源表达；我们发现在Arthrobacter sp. A3体内过表达tpp,可以使该菌0℃时的生存率略有提高。tpp过表达菌株在0℃生存率的提高,以及TPP较低的最适温度水平和低温下保持高催化效率的特征,表明tpp与Arthrobacter sp. A3在低温下生存具有一定相关性。
综上所述,本研究对来源于耐冷节杆菌属TPP进行了首次报道。不仅为节杆菌tpp功能研究提供了科学依据,而且为研究低温菌蛋白以及节杆菌适应低温环境的作用机制奠定了理论基础。
Strains of Arthrobacter are among the most frequently isolated, indigenous, aerobic bacteria found in soils. Members of the genus are known to biodegrade organic compounds in the environment and have the ability to withstand various environmental stresses, such as cold, desiccation, starvation, ionizing radiation, and osmotic stress. The presence of genes for trehalose synthesis in Arthrobacter might be important for this organism's resistance to environmental stresses. The major pathway for trehalose biosynthesis in most organisms involves two enzymes, trehalose-6-phosphate synthase (TPS) and trehalose-6-phosphate phosphatase (TPP). TPP has received great interest because of its abundant biological functions and potential importance for resistance to environmental stresses. Although TPP has been studied in thermophiles and mesophiles, few of them were characterized in cold-adapted microorganisms. A prerequisite for genetic manipulations of these specific genes in Arthrobacter is a high efficiency transformation system that allows for gene cloning, overexpression, and knock-out, as well as for studying trehalose biosynthetic pathway. Thus, in this study, a constitutive gene expression vector pART2 was selected to optimize the electroporation conditions for Arthrobacter sp. A3. Furthermore, the biochemical properties of TPP were studied in this psychrotrophic bacterium. The main results of the present study are as follows:
(1) A simple, rapid, and highly efficient electroporation method which was suitable for Arthrobacter species was established through a systematic examination of the factors involved in the entire electroporation process. Of the parameters assayed, the addition of penicillin to cells during the early log phase of growth and the presence of 0.5 M sorbitol in the electroporation and recovery media produced the greatest increases in transformation efficiency and consistency of results. Using optimum conditions, we generally achieved an efficiency of 6.8 x 10'transformants per microgram of pART2 for Arthrobacter sp. A3. To our knowledge, this level of electro-competence is the highest ever reported for the Arthrobacter genus. The proposed method allows a transformation trial to be accomplished in 10 minutes. This protocol was also successfully applied to other five Arthrobacter species. This method constitutes a useful tool for the genetic manipulations of Arthrobacter, and will facilitate research of this economically important group of organism.
(2) The tpp gene encoding trehalose-6-phosphate phosphatase from Arthrobacter sp. A3 was obtained by thermal asymmetric interlaced PCR (TAIL-PCR). The gene contained a 801-bp open reading frame encoding 266 amino acids. The result of amino acid sequence analysis by bioinformatics showed that there was no signal peptide and transmembrane domain, which indicated that the TPP of Arthrobacter sp. A3 was an intracellular enzyme. BLASTP result revealed that TPP belonged to the HAD superfamily.
(3) The tpp gene was expressed heterogenously in Escherichia coli, and the recombinant enzyme was purified to apparent homogeneity with a calculated molecular weight of 27.9 kDa.
(4) The properties of recombinant TPP were characterized in detail. This enzyme showed an absolute requirement for Mg~(2+)or Co~(2+). The Arthrobacter sp. A3 TPP showed a broad pH optimum range (from pH 5.0 to 7.5), whereas other trehalose-6-phosphate phosphatase characterised do not possess this feature. The temperature optimum was about 30℃, which was also the point of the highest Kcat/Km value (catalytic efficiency) for the recombinant TPP enzyme. The enzyme was stable at low temperatures, as it could maintain 75%of the maximal activity at 4℃. On the other hand, the enzyme was generally heat-labile, losing 70%of its activity when subjected to heat treatment at 50℃for 6 min. The highest Kcat/Km value was 37.5 mM-1·s-1, which was much higher than values published for mesphilic E.coli TPP. The lowest Km value was at 20℃, however, even at 4℃, it possessed the lowest Km value compared to the counterparts from the other reported microorganisms. These characteristics may suggest that this TPP is a novel cold-adapted enzyme.
(5) The tpp gene was expressed homologously in Arthrobacter sp. A3. Overexpression of tpp in Arthrobacter sp. A3 could increase the cell viability slightly at 0℃. The enhancement of viability of tpp-overproducing strain at 0℃, together with the low optimal temperature and the high-catalytic efficiency of TPP at low temperature may indicate that this TPP plays an important role in resistance of Arthrobacter sp. A3 to cold.
This is the first report of the characterization of TPP from psychrotrophic Arthrobacter genus. The research of this paper would provide more knowledge to the functions of TPP, and provide basic information for cold-adapted enzymes, and also provide foundation for further understanding the survival strategies of Arthrobacter at low temperatures.
引文
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