ATP：谷氨酰胺合成酶腺苷酰转移酶活性与谷氨酰胺合成酶去腺苷酸化系统的P1组分的关联。
Association of ATP: glutamine synthetase adenylyltransferase activity with the P1 component of the glutamine synthetase deadenylylation system.
作者信息
Anderson W B, Hennig S B, Ginsburg A, Stadtman E R
出版信息
Proc Natl Acad Sci U S A. 1970 Nov;67(3):1417-24. doi: 10.1073/pnas.67.3.1417.
Abstract
Regulation of glutamine synthetase (EC 6.3.1.2) in Escherichia coli is mediated by adenylylation and deadenylylation of the enzyme. The present studies show that one protein is a common component of both the adenylylation and deadenylylation systems. Thus, the ATP:glutamine synthetase adenylyltransferase, which catalyzes adenylylation of glutamine synthetase, and one of the two proteins required for deadenylylation (the P(I) protein) are inseparable by a variety of fractionation procedures. The adenylyltransferase and P(I)-deadenylylating activities behave as a single protein upon filtration through Agarose A 0.5 gel, and during chromatography on DE32 cellulose and hydroxyapatite columns. They migrate as a single protein band during electrophoresis on polyacrylamide gel and have identical susceptibilities to heat inactivation. These data indicate that the adenylyltransferase and the P(I)-deadenylylation activity are associated with the same protein complex.
摘要
大肠杆菌中谷氨酰胺合成酶（EC 6.3.1.2）的调节是由该酶的腺苷酰化和去腺苷酰化介导的。目前的研究表明，一种蛋白质是腺苷酰化和去腺苷酰化系统的共同组成部分。因此，催化谷氨酰胺合成酶腺苷酰化的ATP：谷氨酰胺合成酶腺苷酰转移酶，以及去腺苷酰化所需的两种蛋白质之一（P(I)蛋白），通过各种分级分离程序都无法分开。腺苷酰转移酶和P(I)去腺苷酰化活性在通过琼脂糖A 0.5凝胶过滤时，以及在DE32纤维素和羟基磷灰石柱色谱过程中，表现为单一蛋白质。它们在聚丙烯酰胺凝胶电泳中迁移为单一蛋白带，并且对热失活具有相同的敏感性。这些数据表明，腺苷酰转移酶和P(I)去腺苷酰化活性与同一蛋白质复合物相关。
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