da Silva A M, Klein C
E. A. Doisy Department of Biochemistry and Molecular Biology, St. Louis University School of Medicine, Missouri 63104.
J Cell Biol. 1990 Aug;111(2):401-7. doi: 10.1083/jcb.111.2.401.
Cells incubated with [3H]myristate were shown to rapidly and specifically acylate a 68-kD protein, p68, in a developmentally-regulated manner. The fatty acid incorporated into p68 was identified as myristate, and is linked to the protein via an amide bond, apparently to an NH2-terminal glycine. The acylation of p68 in D. discoideum displays some unusual properties. Unexpectedly, myristylation of p68 is a posttranslational event and occurs in the presence of inhibitors of protein synthesis. Another unusual finding was that although p68 is a stable protein, the acyl moiety is removed with a half time of approximately 15 min.
用[3H]肉豆蔻酸盐孵育的细胞显示,能以发育调控的方式快速且特异性地将一种68-kD蛋白(p68)酰化。掺入p68的脂肪酸被鉴定为肉豆蔻酸盐,并且通过酰胺键与该蛋白相连,显然是与一个NH2端甘氨酸相连。盘基网柄菌中p68的酰化表现出一些不寻常的特性。出乎意料的是,p68的肉豆蔻酰化是一个翻译后事件,并且在存在蛋白质合成抑制剂的情况下发生。另一个不寻常的发现是,尽管p68是一种稳定的蛋白,但酰基部分以大约15分钟的半衰期被去除。