Interaction of era with the 30S ribosomal subunit: Implications for 30S subunit assembly
Interaction of era with the 30S ribosomal subunit: Implications for 30S subunit assembly
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DOI：
10.1016/j.molcel.2005.03.028
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发表时间：
2005-04-29
期刊：
影响因子：
16
通讯作者：
Agrawal, RK
中科院分区：
文献类型：
--
作者：
Sharma, MR;Barat, C;Agrawal, RK
Era（（E）under bar.大肠杆菌（Ra）中的杆状蛋白）是细菌中高度保守的必需GT3。它与小（30 S）核糖体亚基的16 S核糖体RNA（rRNA）结合，其消耗导致16 S rRNA未加工前体的积累。我们已经获得了一个三维低温电子显微镜图的Thermus thermophilus 30 S-Era复合体。Era结合在30 S亚基的头部和平台之间的裂缝中，并将该亚基锁定在不利于与大（50 S）核糖体亚基缔合的构象中。存在于Era的C-末端结构域内的RNA结合KH基序与16 S rRNA的3'区域中的保守核苷酸相互作用。此外，Era与30 S亚基的几个组装元件接触。这些观察结果表明，直接参与Era的组装和成熟的30 S亚基。
Era ((E) under bar. coli (Ra) under bars-like protein) is a highly conserved and essential GTPase in bacteria. It binds to the 16S ribosomal RNA (rRNA) of the small (30S) ribosomal subunit, and its depletion leads to accumulation of an unprocessed precursor of the 16S rRNA. We have obtained a three-dimensional cryo-electron microscopic map of the Thermus thermophilus 30S-Era complex. Era binds in the cleft between the head and platform of the 30S subunit and locks the subunit in a conformation that is not favorable for association with the large (50S) ribosomal subunit. The RNA binding KH motif present within the C-terminal domain of Era interacts with the conserved nucleotides in the 3' region of the 16S rRNA. Furthermore, Era makes contact with several assembly elements of the 30S subunit. These observations suggest a direct involvement of Era in the assembly and maturation of the 30S subunit.