The human and simian immunodeficiency virus envelope glycoprotein transmembrane subunits are palmitoylated.
The human and simian immunodeficiency virus envelope glycoprotein transmembrane subunits are palmitoylated.
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人类和猿猴免疫缺陷病毒包膜糖蛋白跨膜亚基被棕榈酰化。
DOI：
10.1073/pnas.92.21.9871
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发表时间：
1995
影响因子：
11.1
通讯作者：
Compans,RW
中科院分区：
文献类型：
--
作者：
Yang,C;Spies,CP;Compans,RW
人类免疫缺陷病毒（HIV）和猿猴免疫缺陷病毒（SIV）的包膜蛋白被跨膜蛋白亚基gp41的脂肪酰化修饰。前体gp160在裂解成gp120和gp41亚基之前也被棕榈酰化。棕榈酸标签对羟胺或2-巯基乙醇的处理很敏感，表明这种连接是通过硫酯键进行的。用环己亚胺处理并不能阻止[3H]棕榈酸进入HIV包膜蛋白，这表明棕榈酰化是一种翻译后修饰。与其他糖蛋白不同，HIV-1包膜蛋白的棕榈酰化发生在两个半胱氨酸残基上，Cys-764和Cys-837，它们分别是gp41跨膜结构域的59个和132个氨基酸。序列比较显示，这些残基中的一个（Cys-764）在几乎所有HIV-1分离株的细胞质域中都是保守的，并且位于非常靠近被认为与质膜结合的两亲区。
The envelope proteins of human immunodeficiency virus (HIV) and simian immunodeficiency virus (SIV) were found to be modified by fatty acylation of the transmembrane protein subunit gp41. The precursor gp160 was also palmitoylated prior to its cleavage into the gp120 and gp41 subunits. The palmitic acid label was sensitive to treatment with hydroxylamine or 2-mercaptoethanol, indicating that the linkage is through a thioester bond. Treatment with cycloheximide did not prevent the incorporation of [3H]palmitic acid into the HIV envelope protein, indicating that palmitoylation is a posttranslation modification. In contrast to other glycoproteins, which are palmitoylated at cysteine residues within or close to the membrane-spanning hydrophobic domain, the palmitoylation of the HIV-1 envelope proteins occurs on two cysteine residues, Cys-764 and Cys-837, which are 59 and 132 amino acids, respectively, from the proposed membrane-spanning domain of gp41. Sequence comparison revealed that one of these residues (Cys-764) is conserved in the cytoplasmic domains of almost all HIV-1 isolates and is located very close to an amphipathic region which has been postulated to bind to the plasma membrane.