与特定5S核糖核酸-蛋白质复合物相关的ATP酶和GTP酶活性
ATPase and GTPase activities associated with a specific 5S RNA-protein complex.
作者信息
Horne J R, Erdmann V A
出版信息
Proc Natl Acad Sci U S A. 1973 Oct;70(10):2870-3. doi: 10.1073/pnas.70.10.2870.
Abstract
An RNA-protein complex consisting of 5S RNA and two ribosomal proteins, B-L5 and B-L22, was isolated from Bacillus stearothermophilus ribosomes and found to be active in GTP hydrolysis. This activity was not influenced by elongation factor G. Further analysis of this complex showed that it was also able to hydrolyze ATP. Inhibition studies revealed that ATP was a noncompetitive inhibitor of GTP and that GTP was also a noncompetitive inhibitor of ATP, indicating that two different enzymatic sites were involved. Differences in pH optimum and optimal temperature also point to a twosite enzyme complex. Both enzymatic hydrolyses were inhibited by thiostrepton and fusidic acid, which are known inhibitors of protein synthesis.
摘要
一种由5S RNA以及两种核糖体蛋白B-L5和B-L22组成的RNA-蛋白质复合物，从嗜热脂肪芽孢杆菌核糖体中分离出来，并且发现其具有GTP水解活性。该活性不受延伸因子G的影响。对该复合物的进一步分析表明，它也能够水解ATP。抑制研究显示，ATP是GTP的非竞争性抑制剂，并且GTP也是ATP的非竞争性抑制剂，这表明涉及两个不同的酶位点。最适pH值和最适温度的差异也表明存在双位点酶复合物。两种酶促水解均受到硫链丝菌素和夫西地酸的抑制，这两种物质是已知的蛋白质合成抑制剂。
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