Chattopadhyay S, Das B, Dasgupta C
Department of Biophysics, Molecular Biology and Genetics, University of Calcutta, India.
Proc Natl Acad Sci U S A. 1996 Aug 6;93(16):8284-7. doi: 10.1073/pnas.93.16.8284.
Escherichia coli ribosome, its 50S subunit, or simply the 23S rRNA can reactivate denatured proteins in vitro. Here we show that protein synthesis inhibitors chloramphenicol and erythromycin, which bind to domain V of 23S rRNA of E. coli, can inhibit reactivation of denatured pig muscle lactate dehydrogenase and fungal glucose-6-phosphate dehydrogenase by 23S rRNA completely. Oligodeoxynucleotides complementary to two regions within domain V (which cover sites of chloramphenicol resistant mutations and the putative A site of the incoming aminoacyl tRNA), but not to a region outside of domain V, also can inhibit the activity. Domain V of 23S rRNA, therefore, appears to play a crucial role in reactivation of denatured proteins.
大肠杆菌核糖体、其50S亚基，或者仅仅是23S rRNA在体外均可使变性蛋白质重新激活。在此我们表明，与大肠杆菌23S rRNA结构域V结合的蛋白质合成抑制剂氯霉素和红霉素，可完全抑制23S rRNA对变性猪肌肉乳酸脱氢酶和真菌葡萄糖-6-磷酸脱氢酶的重新激活作用。与结构域V内两个区域（涵盖氯霉素抗性突变位点和即将进入的氨酰tRNA的假定A位点）互补，但与结构域V外的一个区域不互补的寡脱氧核苷酸，也可抑制该活性。因此，23S rRNA的结构域V似乎在变性蛋白质的重新激活中起关键作用。
