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首页> 外文期刊>Protein Science: A Publication of the Protein Society >Fluorescence resonance energy transfer study of subunit exchange in human lens crystallins and congenital cataract crystallin mutants.
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Fluorescence resonance energy transfer study of subunit exchange in human lens crystallins and congenital cataract crystallin mutants.

机译：人类晶状体晶状体蛋白和先天性白内障晶状体蛋白突变体中亚基交换的荧光共振能量转移研究。

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摘要

Lens alpha-crystallin is an oligomeric protein with a molecular mass of 500-1000 kDa and a polydispersed assembly. It consists of two types of subunits, alphaA and alphaB, each with a molecular mass of 20 kDa. The subunits also form homo-oligomers in some other tissues and in vitro. Their quaternary structures, which are dynamic and characterized by subunit exchange, have been studied by many techniques, including fluorescence resonance energy transfer (FRET) and mass spectrometry analysis. The proposed mechanism of subunit exchange has been either by dissociation/association of monomeric subunits or by rapid equilibrium between oligomers and suboligomers. To explore the nature of subunit exchange further, we performed additional FRET measurements and analyses using a fluorescent dye-labeled W9F alphaA-crystallin as the acceptor probe and Trp in other crystallins (wild-type and R116C alphaA, wild-type and R120G alphaB, wild-type and Q155* betaB2) as the donor probe and calculated the transfer efficiency, Forster distance, and average distance between two probes. The results indicate only slight decreased efficiency and increased distance between two probes for the R116C alphaA and R120G alphaB mutations despite conformational changes.
机译：晶状体α-晶状体蛋白是一种寡聚蛋白，分子量为500-1000 kDa，具有多分散的组装体。它由两种类型的亚基，即alphaA和alphaB组成，每种亚基的分子质量均为20 kDa。亚基还可以在其他一些组织中和体外形成同源寡聚体。它们的四级结构是动态的，具有亚基交换特征，已经通过许多技术进行了研究，包括荧光共振能量转移（FRET）和质谱分析。所提出的亚基交换机制是通过单体亚基的解离/缔合或通过低聚物与亚低聚物之间的快速平衡来实现的。为了进一步探讨亚基交换的性质，我们使用荧光染料标记的W9F alphaA-crystallin作为受体探针并在其他crystallins（野生型和R116C alphaA，野生型和R120G alphaB，野生型和Q155 * betaB2）作为供体探针，并计算了转移效率，Forster距离和两个探针之间的平均距离。结果表明，尽管构象发生了变化，但对于R116C alphaA和R120G alphaB突变，两个探针之间的效率只有轻微降低，距离增加了。

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