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首页> 外文期刊>Biochemistry >Thermal unfolding of three acclimation temperature-associated isoforms of carp light meromyosin expressed by recombinant DNAs
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Thermal unfolding of three acclimation temperature-associated isoforms of carp light meromyosin expressed by recombinant DNAs

机译：重组DNA表达的三种与鲤鱼轻肌球蛋白适应温度相关的亚型的热解

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Differential scanning calorimetry (DSC) was performed to investigate thermodynamic properties of three carp fast skeletal light meromyosin (LMM) isoforms expressed in Escherichia coli by recombinant DNAs. Three isoforms were the 10 degrees C-, intermediate-, and 30 degrees C-type LMM predominantly expressed in carp acclimated to 10, 20, and 3 degrees C. The isoforms expressed in E. coli by recombinant DNAs exhibited a typical pattern of alpha-helix in CD spectroscopy with two minima at 222 and 208 nm, Moreover, the three isoforms formed paracrystals typical of LMM, suggesting that expressed proteins retained intact structural properties. When the LMM isoforms were subjected to DSC analysis, the 10 degrees C and 30 degrees C types showed endotherms having transition temperatures (T-m) at 35.1 and 39.5 degrees C, respectively, which are responsible for thermal unfolding of alpha-helix. The intermediate type exhibited two comparable endotherms with T-m values at 34.9 and 40.6 degrees C, implying that it has intermediate thermodynamic properties between those of 10 degrees C and 30 degrees C types. However, a chimeric LMM having the 10 degrees C and 30 degrees C type as N- and C-terminal halves, respectively, showed the DSC pattern typical of the whole 30 degrees C-type molecule. On the other hand, another chimeric LMM composed of the N-terminal 30 degrees C type and C-terminal 10 degrees C type gave the pattern of the full 10 degrees C type. These results suggest that thermodynamic properties of the C-terminal half largely account for thermal unfolding of the whole molecule. [References: 40]
机译：进行差示扫描量热法（DSC）来研究重组DNA在大肠杆菌中表达的三种鲤鱼快速骨骼肌轻肌球蛋白（LMM）亚型的热力学性质。三种同工型是10℃，中型和30℃型LMM，主要在适应10、20和3℃的鲤鱼中表达。重组DNA在大肠杆菌中表达的同工型表现出典型的α模式在CD光谱中呈螺旋形，在222和208 nm处有两个最小值，此外，这三个同工型形成了LMM的典型副晶体，表明表达的蛋白质保留了完整的结构特性。当对LMM同工型进行DSC分析时，10℃和30℃类型的吸热曲线分别具有35.1和39.5℃的转变温度（T-m），这是α螺旋热展开的原因。中间类型表现出两个可比较的吸热峰，它们的T-m值分别为34.9和40.6摄氏度，这意味着它具有介于10摄氏度和30摄氏度之间的中间热力学性质。但是，分别具有10摄氏度和30摄氏度类型的N和C端半部分的嵌合LMM显示了整个30摄氏度类型分子典型的DSC模式。另一方面，由N末端30℃型和C末端10℃型组成的另一嵌合LMM给出了全10℃型的图案。这些结果表明，C末端一半的热力学性质在很大程度上解释了整个分子的热展开。 [参考：40]

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