Lipid-binding properties of TRIM72
Lipid-binding properties of TRIM72
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DOI：
10.5483/bmbrep.2012.45.1.26
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发表时间：
2012-01-31
期刊：
影响因子：
3.8
通讯作者：
Park, Heonyong
中科院分区：
文献类型：
--
作者：
Kim, Sunghyen;Seo, Jeonghwa;Park, Heonyong
已知TRIM72在骨骼肌膜修复中起关键作用。为了更好地了解该蛋白的分子机制，我们进行了与TRIM72的体外结合研究。我们的研究证明，TRIM72能与多种脂类结合，其解离常数(K-d)介于88.2nM/-9.9nM到550.5+/-134.5 nM之间。此外，当蛋白被搅拌稀释时，TRIM72的本征荧光呈指数下降。时间分辨的荧光衰减与浓度无关。荧光衰变的TRIM72仍保持其二级结构，但其结合性能显著降低。荧光衰减的TRIM72对棕榈酸酯和硬脂酸酯的解离常数分别为159.1+/-39.9nM和355.4+/-106.0 nM。这项研究表明，TRIM72可以被各种刺激动态转换。这项研究的结果也为TRIM72在肌膜损伤修复中的作用提供了深入的了解。(BMB报告2012；45(1)：26-31)
TRIM72 is known to play a critical role in skeletal muscle membrane repair. To better understand the molecular mechanisms of this protein, we carried out an in vitro binding study with TRIM72. Our study proved that TRIM72 binds various lipids with dissociation constants (K-d) ranging from 88.2 +/- 9.9 nM to 550.5 +/- 134.5 nM. In addition, the intrinsic fluorescence of TRIM72 exponentially decreased when the protein was diluted with stirring. The time-resolved fluorescence decay occurred in a concentration-independent manner. The fluorescence-decayed TRIM72 remained in its secondary structure, but its binding properties were significantly reduced. The dissociation constants (K-d) of fluorescence-decayed TRIM72 for palmitate and stearate were 159.1 +/- 39.9 nM and 355.4 +/- 106.0 nM, respectively. This study suggests that TRIM72 can be dynamically converted by various stimuli. The results of this study also provide insight into the role of TRIM72 in the repair of sarcolemma damage. (BMB reports 2012; 45(1): 26-31)