ADP-RIBOSYLATION OF MEMBRANE PROTEINS CATALYZED BY CHOLERA TOXIN - BASIS OF ACTIVATION OF ADENYLATE-CYCLASE
ADP-RIBOSYLATION OF MEMBRANE PROTEINS CATALYZED BY CHOLERA TOXIN - BASIS OF ACTIVATION OF ADENYLATE-CYCLASE
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DOI：
10.1073/pnas.75.7.3050
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发表时间：
1978-01-01
影响因子：
11.1
通讯作者：
MEREN, R
中科院分区：
文献类型：
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作者：
GILL, DM;MEREN, R
在ATP和胞质因子的存在下，霍乱毒素片段A1催化ADP-核糖从NAD转移到鸽子红细胞的许多可溶性和膜结合蛋白。证据表明，最容易修改的膜蛋白（MW 42,000）是腺苷酸环化酶相关的GTP结合蛋白。它被毒素修饰是由鸟嘌呤核苷酸刺激的。腺苷酸环化酶的活性增加与ADP-核糖添加到该蛋白质平行，并减少与随后的逆转ADP-核糖基化毒素和烟酰胺。如果红细胞溶解，则该蛋白质仅可接近毒素A亚基。当腺苷酸环化酶活性达到最大值时，与该蛋白质结合的ADP-核糖残基的数目（约1500个/细胞）与报道的β-腺苷酸环化酶的数目相似。肾上腺素能受体
In the presence of ATP and a cytosolic factor, cholera toxin fragment A1 catalyzes the transfer of ADP-ribose from NAD to a number of soluble and membrane-bound proteins of the pigeon erythrocyte. Evidence is presented that suggests that the most readily modified membrane protein (MW 42,000) is the adenylate cyclase-associated GTP-binding protein. Its modification by toxin is stimulated by guanine nucleotides. Adenylate cyclase activity increases in parallel with the addition of ADP-ribose to this protein and decreases in parallel with the subsequent reversal of ADP-ribosylation by toxin and nicotinamide. The protein is only accessible to toxin A subunits if the erythrocytes are lysed. When adenylate cyclase activity reaches a maximum, the number of ADP-ribose residues bound to this protein (about 1500/cell) is similar to the reported number of .beta.-adrenergic receptors.