Trompier Doriane, Alibert Mélanie, Davanture Suzel, Hamon Yannick, Pierres Michel, Chimini Giovanna
Centre d'Immunologie de Marseille-Luminy, INSERM, CNRS, UniversitédelaMéditerranée, Parc Scientifique de Luminy, 13288 Marseille Cedex 09, France.
J Biol Chem. 2006 Jul 21;281(29):20283-90. doi: 10.1074/jbc.M601072200. Epub 2006 May 18.
Fluorescence resonance energy transfer and native PAGE analytical techniques were employed to assess the quaternary structure of ABCA1, an ATP binding cassette transporter playing a crucial role in cellular lipid handling. These experimental approaches support the conclusion that ABCA1 is associated in dimeric structures that undergo transition into higher order structures, i.e. tetramers, during the ATP catalytic cycle. Our data hence underline molecular assembly as a crucial parameter in ABCA1 function and the advantage of native PAGE as analytical tool for intractable membrane proteins.
采用荧光共振能量转移和天然聚丙烯酰胺凝胶电泳分析技术来评估ABCA1的四级结构，ABCA1是一种ATP结合盒转运蛋白，在细胞脂质处理中起关键作用。这些实验方法支持以下结论：ABCA1以二聚体结构存在，在ATP催化循环过程中会转变为更高阶的结构，即四聚体。因此，我们的数据强调了分子组装是ABCA1功能的关键参数，以及天然聚丙烯酰胺凝胶电泳作为分析难处理膜蛋白的工具的优势。
