豌豆肌动蛋白异型体（PEAc1）的原核表达及其藻荧光探针的研制
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摘要
肌动蛋白在真核生物中广泛存在，由肌动蛋白参与形成的动态微丝骨架系统是细胞生命活动的基础。在植物细胞中，肌动蛋白由多基因家族编码，从而产生了多种肌动蛋白异型体。肌动蛋白异型体在植物体内的表达具有组织特异性，在植物生长发育的不同阶段具有不同的表达模式，从而发挥不同的功能，它们与众多肌动蛋白结合蛋白也具有不同的相互作用。因此，体外研究植物肌动蛋白异型体理化特性将对深入了解它们在体内的功能及其动态调节具有重要意义。荧光标记技术虽然广泛用于细胞内微丝骨架分布及其动态的研究，但传统的荧光标记方法用于植物肌动蛋白研究时都具有一定的局限性，利用GFP融合以及研制新型的藻荧光探针有助于对植物肌动蛋白的深入了解。
利用基因融合技术，原核表达并从包涵体中纯化了豌豆肌动蛋白异型体PEAc1、His-tagged PEAc1、His-tagged GFP以及His-tagged PEAc1-GFP，并通过诱导条件的筛选达到了可溶性表达与大量纯化His-tagged PEAc1-GFP的目的。利用圆二色谱法对肌动蛋白二级结构的测定表明：与预测值相比，可溶性表达与纯化的His-tagged PEAc1-GFP具有更为合理的二级结构，His-GFP-tag的融合促进了PEAc1的可溶性表达与正确折叠。这一方法可能是解决植物肌动蛋白及其他在包涵体中表达蛋白难以正确折叠和大量纯化的有效途径之一。
对纯化的上述肌动蛋白的聚合活性进行了详细研究。荧光标记结合荧光显微观察表明：从可溶性上清中纯化的His-tagged PEAc1-GFP聚合形成的微丝不仅可以直接在荧光显微镜下观察，也可被微丝的特异标记物鬼笔环肽所标记，而且其直径、长度以及形态上与已知的聚合肌动蛋白荧光丝一致；电镜负染的结果进一步证实其直径为9nm，与传统微丝直径相当(7—10nm)；聚合曲线有明显的停滞期，为典型的S型聚合曲线，聚合临界浓度为0.75μmol／L，这一结果与已有报道相似。上述结果表明，通过GFP的融合而在大肠杆菌中可溶性表达的PEAc1，不仅很好保持了肌动蛋白的聚合活性，而且GFP的荧光特性也方便了微丝体外特性的研究。
通过肌动蛋白体外对DNase Ⅰ以及肌球蛋白ATPase活性影响的研究，发现单体His-tagged PEAc1-GFP能显著抑制DNase Ⅰ活性，在肌动蛋白聚合条件下能有效激活肌球蛋白ATPase活性，这一结果预示着PEAc1在体内可能参与相关的生命活动，为利用GFP直接与肌动蛋白异型体融合来研究体内微丝的动态变化及其调节提供了实验依据。
以原核表达的PEAc1为抗原制备了免疫活性较好的抗豌豆肌动蛋白的多克隆抗体，从螺旋藻中纯化了高纯度、高活性、能结晶的藻胆蛋白，将两者偶联制备的藻荧光探针，不仅保持了藻胆蛋白很强的抗荧光淬灭能力，而且用于豌豆卷须气孔细胞荧光标记时有更低的荧光背景。对豌豆肌动蛋白藻荧光探针的初步研究，不仅为豌豆肌动蛋白的免疫荧光检测提供了便利条件，而且通过改变抗体，则可以将藻荧光探针用于其他植物蛋白的标记，藻荧光探针优越的荧光特性使其在植物材料的免疫荧光检测中具有广阔的应用前景。对藻蓝蛋白两个亚基基因的克隆、原核表达与纯化及其荧光特性恢复的初步研究为优化藻荧光探针及拓宽其应用范围提供了一定的实验依据。
Actin, the major component of the dynamic microfilaments system, exists in nearly all eukaryotic cells, and plays an essential role in living activities. In plants, actins are encoded by multi-gene families. There are many kinds of actin isoforms expressed in tissue-specificity and different phases during plant development for different functions. Actin isoforms have complicated interactions with actin-binding proteins. So it is important to study the physicochemical properties of plant actin isoforms in vitro for further understanding their functions and dynamic regulation in vivo. Although fluorescence labeling method was widely used in the observation of microfilaments' dynamic distributions in vivo, all of the traditional methods have their limits. The use of GFP fusion and the preparation of new type of algae fluorescent probe will facilitate our further study on plant actins.
By gene fusion and prokaryotic expression, we purified a pea actin isoform (PEAc1), His-tagged PEAc1, His-tagged GFP and His-tagged PEAc1-GFP from inclusion body. After filtrating a series of induction condition, we expressed and purified His-tagged PEAc1 with soluble form in a large amount. The secondary structure of fusion proteins was determined by circular dichroism spectrum (CD). Compared with the results predicted with biology software, His-tagged PEAc1-GFP expressed in soluble form has more reasonable secondary structure, indicating that the fusion of His-GFP-tag facilitates PEAcl's soluble expression and correct folding. This may be a good method for obtaining soluble and abundant plant actin isoforms and other proteins which could not fold exactly and exist in inclusion body by prokaryotic expression.
The polymerization ability of the fusion actins above was studied in detail. The his-tagged PEAcl-GFP purified from the supernatants could polymerize into green fluorescent filamentous structures with diameter, length and shape being identical to that of muscle F-actins, which could be labeled by TRITC-phalloidin (a specific agent for staining actin microfilaments), and were identified as having a 9 nm diameter by negative staining, corresponding with that of the muscle F-actins (7-10 nm). Under polymerization conditions, His-tagged PEAcl-GFP polymerized with kinetics similar to those of skeleton muscle actin, that is, an obvious lag nucleation period at the beginning of polymerization and an S-like typical polymerization curve could be obtained. The critical concentration is 0.75 umol/L near to that of chicken muscle actin (0.56 umol/L) under the same condition. All above showed that PEAcl preserved the polymerization activities of actin, and GFP fusion gave facilities for the study of microfilaments proper
ties in vitro.
Monomer His-tagged PEAc1-GFP could notably inhibit DNase I activities. Polymer His-tagged PEAc1-GFP efficiently activated myosin Mg-ATPase activity, which indicated that PEAcl might take part in correlative living activities in vivo. Moreover, this result provided experimental proof in vitro for fusing GFP to actin isoform directly to study the dynamics of microfilaments and its regulation in vivo.
We prepared rabbit anti-pea actins polyclonal antibodies using PEAcl as antigen which being expressed and purified from prokaryotic cells, and the antibodies possessed better immunity activity to pea actins. .From the direct mutant of Spirulina platensis(SP-D), we got high purity and activity
phycobiliprotein which could grow crystals. The algae fluorescent probe prepared by coupling the above polyclonal antibody to phycobilipotein not only keeps the property of stronger anti-fluorescence quenching but also has the lower fluorescent background when it was used for labeling stoma cells of pea tendril. The data above showed that algae phycobiliprotein fluorescent probes not only facilitate the study to pea actins but also provide a doable method to label other plant proteins. It has a good foreground for algae fluorescence probe to be used in the immunity fluorescent detection of plant cells. The gene clon
利用基因融合技术，原核表达并从包涵体中纯化了豌豆肌动蛋白异型体PEAc1、His-tagged PEAc1、His-tagged GFP以及His-tagged PEAc1-GFP，并通过诱导条件的筛选达到了可溶性表达与大量纯化His-tagged PEAc1-GFP的目的。利用圆二色谱法对肌动蛋白二级结构的测定表明：与预测值相比，可溶性表达与纯化的His-tagged PEAc1-GFP具有更为合理的二级结构，His-GFP-tag的融合促进了PEAc1的可溶性表达与正确折叠。这一方法可能是解决植物肌动蛋白及其他在包涵体中表达蛋白难以正确折叠和大量纯化的有效途径之一。
对纯化的上述肌动蛋白的聚合活性进行了详细研究。荧光标记结合荧光显微观察表明：从可溶性上清中纯化的His-tagged PEAc1-GFP聚合形成的微丝不仅可以直接在荧光显微镜下观察，也可被微丝的特异标记物鬼笔环肽所标记，而且其直径、长度以及形态上与已知的聚合肌动蛋白荧光丝一致；电镜负染的结果进一步证实其直径为9nm，与传统微丝直径相当(7—10nm)；聚合曲线有明显的停滞期，为典型的S型聚合曲线，聚合临界浓度为0.75μmol／L，这一结果与已有报道相似。上述结果表明，通过GFP的融合而在大肠杆菌中可溶性表达的PEAc1，不仅很好保持了肌动蛋白的聚合活性，而且GFP的荧光特性也方便了微丝体外特性的研究。
通过肌动蛋白体外对DNase Ⅰ以及肌球蛋白ATPase活性影响的研究，发现单体His-tagged PEAc1-GFP能显著抑制DNase Ⅰ活性，在肌动蛋白聚合条件下能有效激活肌球蛋白ATPase活性，这一结果预示着PEAc1在体内可能参与相关的生命活动，为利用GFP直接与肌动蛋白异型体融合来研究体内微丝的动态变化及其调节提供了实验依据。
以原核表达的PEAc1为抗原制备了免疫活性较好的抗豌豆肌动蛋白的多克隆抗体，从螺旋藻中纯化了高纯度、高活性、能结晶的藻胆蛋白，将两者偶联制备的藻荧光探针，不仅保持了藻胆蛋白很强的抗荧光淬灭能力，而且用于豌豆卷须气孔细胞荧光标记时有更低的荧光背景。对豌豆肌动蛋白藻荧光探针的初步研究，不仅为豌豆肌动蛋白的免疫荧光检测提供了便利条件，而且通过改变抗体，则可以将藻荧光探针用于其他植物蛋白的标记，藻荧光探针优越的荧光特性使其在植物材料的免疫荧光检测中具有广阔的应用前景。对藻蓝蛋白两个亚基基因的克隆、原核表达与纯化及其荧光特性恢复的初步研究为优化藻荧光探针及拓宽其应用范围提供了一定的实验依据。
Actin, the major component of the dynamic microfilaments system, exists in nearly all eukaryotic cells, and plays an essential role in living activities. In plants, actins are encoded by multi-gene families. There are many kinds of actin isoforms expressed in tissue-specificity and different phases during plant development for different functions. Actin isoforms have complicated interactions with actin-binding proteins. So it is important to study the physicochemical properties of plant actin isoforms in vitro for further understanding their functions and dynamic regulation in vivo. Although fluorescence labeling method was widely used in the observation of microfilaments' dynamic distributions in vivo, all of the traditional methods have their limits. The use of GFP fusion and the preparation of new type of algae fluorescent probe will facilitate our further study on plant actins.
By gene fusion and prokaryotic expression, we purified a pea actin isoform (PEAc1), His-tagged PEAc1, His-tagged GFP and His-tagged PEAc1-GFP from inclusion body. After filtrating a series of induction condition, we expressed and purified His-tagged PEAc1 with soluble form in a large amount. The secondary structure of fusion proteins was determined by circular dichroism spectrum (CD). Compared with the results predicted with biology software, His-tagged PEAc1-GFP expressed in soluble form has more reasonable secondary structure, indicating that the fusion of His-GFP-tag facilitates PEAcl's soluble expression and correct folding. This may be a good method for obtaining soluble and abundant plant actin isoforms and other proteins which could not fold exactly and exist in inclusion body by prokaryotic expression.
The polymerization ability of the fusion actins above was studied in detail. The his-tagged PEAcl-GFP purified from the supernatants could polymerize into green fluorescent filamentous structures with diameter, length and shape being identical to that of muscle F-actins, which could be labeled by TRITC-phalloidin (a specific agent for staining actin microfilaments), and were identified as having a 9 nm diameter by negative staining, corresponding with that of the muscle F-actins (7-10 nm). Under polymerization conditions, His-tagged PEAcl-GFP polymerized with kinetics similar to those of skeleton muscle actin, that is, an obvious lag nucleation period at the beginning of polymerization and an S-like typical polymerization curve could be obtained. The critical concentration is 0.75 umol/L near to that of chicken muscle actin (0.56 umol/L) under the same condition. All above showed that PEAcl preserved the polymerization activities of actin, and GFP fusion gave facilities for the study of microfilaments proper
ties in vitro.
Monomer His-tagged PEAc1-GFP could notably inhibit DNase I activities. Polymer His-tagged PEAc1-GFP efficiently activated myosin Mg-ATPase activity, which indicated that PEAcl might take part in correlative living activities in vivo. Moreover, this result provided experimental proof in vitro for fusing GFP to actin isoform directly to study the dynamics of microfilaments and its regulation in vivo.
We prepared rabbit anti-pea actins polyclonal antibodies using PEAcl as antigen which being expressed and purified from prokaryotic cells, and the antibodies possessed better immunity activity to pea actins. .From the direct mutant of Spirulina platensis(SP-D), we got high purity and activity
phycobiliprotein which could grow crystals. The algae fluorescent probe prepared by coupling the above polyclonal antibody to phycobilipotein not only keeps the property of stronger anti-fluorescence quenching but also has the lower fluorescent background when it was used for labeling stoma cells of pea tendril. The data above showed that algae phycobiliprotein fluorescent probes not only facilitate the study to pea actins but also provide a doable method to label other plant proteins. It has a good foreground for algae fluorescence probe to be used in the immunity fluorescent detection of plant cells. The gene clon
引文
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