Mannella C A
Wadsworth Center for Laboratories and Research, State University of New York, Albany 12201.
J Ultrastruct Mol Struct Res. 1988 Feb;98(2):212-6. doi: 10.1016/s0889-1605(88)80912-1.
The channel protein in the mitochondrial outer membrane of Neurospora crassa aggregates laterally into crystalline arrays by the action of phospholipase A2. When mitochondrial outer membranes are reacted with filipin and examined by negative-stain electron microscopy, filipin-sterol complexes are found everywhere on the membranes except on the crystalline channel arrays. This suggests that the channel-rich membrane domains may have a relatively low content of accessible sterol. It is proposed that in vitro segregation of protein and lipid membrane components by phospholipase A2 may reflect a mechanism by which the endogenous enzyme organizes the native mitochondrial membrane into functional domains.
粗糙脉孢菌线粒体外膜中的通道蛋白在磷脂酶A2的作用下横向聚集成晶体阵列。当线粒体外膜与制霉菌素反应并通过负染色电子显微镜检查时，除了晶体通道阵列外，在膜上各处都发现了制霉菌素 - 甾醇复合物。这表明富含通道的膜结构域可能具有相对较低的可及甾醇含量。有人提出，磷脂酶A2在体外对蛋白质和脂质膜成分的分离可能反映了一种内源性酶将天然线粒体膜组织成功能结构域的机制。
