A novel GTPase activated by the small subunit of ribosome
A novel GTPase activated by the small subunit of ribosome
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DOI：
10.1093/nar/gkh861
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发表时间：
2004-01-01
影响因子：
14.9
通讯作者：
Muto, A
中科院分区：
文献类型：
--
作者：
Himeno, H;Hanawa-Suetsugu, K;Muto, A
大肠杆菌YjeQ的GTP酶活性，在此称为RsgA（核糖体小亚基依赖性GTP酶A），已显示核糖体或其小亚基显著增强。几种氨基糖苷类结合在小亚基的A位点，但不是由P位点特异性抗生素的抑制GTcirp活性的增强。RsgA在GDPNP存在下稳定结合小亚基，但在GTP或GDP存在下不结合，以将核糖体解离成亚基。从基因组中破坏RsgA的基因影响细胞的生长，所述细胞主要含有仅具有弱的RsgA活化活性的解离亚基。我们还发现，17S RNA，一个假定的前体16S rRNA，包含在核糖体的小亚基从RsgA缺失菌株。RsgA是一种新的GTdR，它可能为研究核糖体的功能提供新的视角。
The GTPase activity of Escherichia coli YjeQ, here named RsgA (ribosome small subunit-dependent GTPase A), has been shown to be significantly enhanced by ribosome or its small subunit. The enhancement of GTPase activity was inhibited by several aminoglycosides bound at the A site of the small subunit, but not by a P site-specific antibiotic. RsgA stably bound the small subunit in the presence of GDPNP, but not in the presence of GTP or GDP, to dissociate ribosome into subunits. Disruption of the gene for RsgA from the genome affected the growth of the cells, which predominantly contained the dissociated subunits having only a weak activation activity of RsgA. We also found that 17S RNA, a putative precursor of 16S rRNA, was contained in the small subunit of the ribosome from the RsgA-deletion strain. RsgA is a novel GTPase that might provide a new insight into the function of ribosome.