Fatty acid acylation of eucaryotic cell membrane proteins.
Fatty acid acylation of eucaryotic cell membrane proteins.
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真核细胞膜蛋白的脂肪酸酰化。
DOI：
10.1016/0304-4157(82)90008-9
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发表时间：
1982
期刊：
影响因子：
--
通讯作者：
Schlesinger,MJ
中科院分区：
文献类型：
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作者：
Magee,AI;Schlesinger,MJ
许多处于“成熟”功能状态的蛋白质的一级结构包括各种化学取代基，这些取代基被添加到蛋白质的多肽骨架上。其中包括低聚糖、磷酸、甲基和核苷，它们与多肽的添加既发生在新生链生物合成过程中，也发生在蛋白质整合到细胞代谢活动中时。很明显，蛋白质的氨基酸序列和编码它们的基因是控制这种修饰的主要决定因素，但这些修饰如何影响功能只在少数情况下才确切知道。在这篇综述中，我们讨论了一种似乎影响真核细胞中某些蛋白质与膜相互作用的修饰。这里的取代基是脂肪酸，直到最近，关于它们与蛋白质的共价结合的知识仅限于少数高度专门化的细菌蛋白(见参考文献[1])。1)。布劳恩[2]在大肠杆菌细胞壁中发现了一种‘脂蛋白’，这导致了详细的结构研究，表明脂肪酸与蛋白质的酯和酰胺键结合在一起[3]。酯化的脂肪酸连接到甘油部分，甘油部分以硫醚的形式连接到氨基末端的半胱氨酸，而第三种脂肪酸结合在末端的氨基上。最近，地衣芽孢杆菌的膜青霉素酶被证明含有脂肪酸和甘油，其连接类似于大肠杆菌蛋白[4-7]。30多年前，Folch-Pi和Lees在分析脑髓鞘中有机溶剂可提取的蛋白质时首次报道了高等生物体中可能存在的脂类与蛋白质的共价结合[8，9]。大约3年前，对一种被包裹的动物病毒的两种糖蛋白的研究表明，这些膜相关蛋白也含有共价结合的脂肪酸[10，13]。目前，有大量来自包膜病毒、组织培养细胞和动物细胞的膜蛋白
The primary structure of many proteins in their'mature'functional state includes various kinds of chemical substituents that have been added onto the protein's polypeptide backbone. Among these are oligosaccharides, phosphate, methyl groups, and nucleosides and their addition to the polypeptide occurs both during nascent chain biosynthesis and later as the protein becomes integrated into cellular metabolic activity. It is clear that a protein's sequence of amino acids and the gene encoding them is the primary determining factor in controlling such modifications, but precisely how these modifications affect function is known in only a few cases. In this review, we discuss a modification that appears to influence the interaction of some proteins with membranes in eukaryotic cells. The substituents here are fatty acids and, until recently, knowledge of their covalent attachment to proteins was limited to a small number of highly specialized bacterial proteins (reviewed in Ref. 1). The discovery by Braun [2] of a'lipoprotein'in the Escherichia coli cell wall led to detailed structural studies which showed that fatty acids were bound in both ester and amide linkages to the protein [3]. The esterified fatty acids were attached to a glycerol moiety that was in thioether linkage to the amino terminal cysteine while a third fatty acid was bound to the terminal a amino group. More recently, the membrane penicillinase of Bacillus licheniformis has been shown to contain fatty acids and glycerol in linkages analogous to the E. coli protein [4-7]. The possible covalent attachment of lipid to proteins in higher organisms was first reported over 30 years ago by Folch-Pi and Lees in their analysis of an organic-solvent extractable protein from brain myelin [8, 9]. About 3 years ago, studies of two glycoproteins from an enveloped animal virus suggested that these membrane-associated proteins also contained covalently-bound fatty acids [10, 13]. Presently, there are a substantial number of membrane proteins from enveloped viruses, tissue culture cells, and animal cells that