Stark M J, Cundliffe E, Dijk J, Stöffler G
Mol Gen Genet. 1980;180(1):11-5. doi: 10.1007/BF00267346.
Ribosomes from the thiostrepton-resistant mutant MJ1 of Bacillus megaterium completely lack a protein designated BM-L11. When assayed in vitro, such ribosomes show an impaired ability to hydrolyse GTP in the presence of the elongation factor EF-G and are unable to support the synthesis of (p)ppGpp in response to the stringent factor. Restoration of both these activities can be achieved by re-addition of either protein BM-L11 or its serological homologue from Escherichia coli, protein L11, implying that these two proteins are related functionally as well as immunologically.
巨大芽孢杆菌硫链丝菌素抗性突变体MJ1的核糖体完全缺乏一种名为BM-L11的蛋白质。在体外检测时,此类核糖体在延伸因子EF-G存在的情况下水解GTP的能力受损,并且在受到严谨因子作用时无法支持(p)ppGpp的合成。通过重新添加蛋白质BM-L11或其来自大肠杆菌的血清学同源物蛋白质L11,这两种活性均可恢复,这意味着这两种蛋白质在功能上以及免疫学上均相关。