Protein-lipid interactions of the proteolipid c subunit of the Escherichia coli proton-translocating adenosinetriphosphatase.
Protein-lipid interactions of the proteolipid c subunit of the Escherichia coli proton-translocating adenosinetriphosphatase.
复制标题
大肠杆菌质子转位腺苷三磷酸酶蛋白脂质 c 亚基的蛋白质-脂质相互作用。
DOI：
10.1006/abbi.1993.1395
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发表时间：
1993
影响因子：
3.9
通讯作者：
Brusilow,WS
中科院分区：
文献类型：
--
作者：
Ksenzenko,SM;Brusilow,WS
Escherichia colimembrane磷脂与F1F0质子转运ATP酶的疏水性C亚基之间的相互作用的特点。E.用氯仿和甲醇的中性混合物和随后的分离步骤制备几种含蛋白质的级分。最可溶于有机溶剂中的含蛋白质馏分含有亚基c和脂质馏分相比，总磷脂酰甘油丰富。肠膜磷脂通过这种方法从膜中提取的其他ATP酶亚基和一些额外的蛋白质可以通过随后的提取与c亚基分离。纯化和脱脂的c亚基含有脂肪酸，其在用三氟化硼甲醇处理后释放。此外，删除和恢复F0亚基的基因改变了可提取的膜磷脂和脂肪酸的组成，表明F0在膜中起着重要的结构作用。
Interactions betweenEscherichia colimembrane phospholipids and the hydrophobic c subunit of the F1F0proton-translocating ATPase were characterized. Extraction ofE. colimembranes with a neutral mixture of chloroform and methanol and subsequent separation steps produced several protein-containing fractions. The protein-containing fraction most soluble in organic solvents contained subunit c and a lipid fraction enriched in phosphatidylglycerol compared to totalE. colimembrane phospholipids. Other ATPase subunits and some additional proteins extracted from the membranes by this procedure could be separated from the c subunit by subsequent extraction. The purified and delipidated c subunit contained fatty acids which were released upon treatment with boron trifluoride methanol. Furthermore, deleting and restoring the genes for the F0subunits changed the composition of extractable membrane phospholipid and fatty acids, indicating that the F0plays a significant structural role in the membrane.