STRUCTURAL INVESTIGATION OF PHE TRANSFER RNAPHE FROM ESCHERICHIA-COLI BOUND TO THE RIBOSOMAL A-SITE
STRUCTURAL INVESTIGATION OF PHE TRANSFER RNAPHE FROM ESCHERICHIA-COLI BOUND TO THE RIBOSOMAL A-SITE
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DOI：
10.1093/nar/11.3.575
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发表时间：
1983-01-01
影响因子：
14.9
通讯作者：
WAGNER, R
中科院分区：
文献类型：
--
作者：
BERTRAM, S;GORINGER, U;WAGNER, R
phe- trnapheme中鸟苷的酮醛修饰。大肠杆菌研究了游离状态的tRNA，并特异性结合到核糖体a位点。与核糖体形成的复合体保护了tRNA分子中两个遥远位点的化学修饰。受影响的鸟苷是位于d环的G-18和G-19，以及位于反密码子环的G-34。在核糖体缺失的情况下对phetrnaphein的修饰导致tRNA结构的不稳定。我们的数据与结论一致，即在反密码子环上改变G-34会引发tRNA分子远端的构象不稳定。
SUMMARYKethoxal modification of guanosines within phe-tRNAphefromE.Coliwas studied for tRNA in the free state and specifically bound to the ribosomal A-site. Complex formation with the ribosome results in a protection from chemical modification of two distant sites in the tRNA molecule. The guanosines affected are G-18 and G-19, located in the D-loop, and G-34 in the anticodon loop.Modification of phe-tRNAphein the absence of ribosomes leads to a destabilisation of the tRNA structure. Our data are consistent with the conclusion that mocification of G-34 at the anticodon loop triggers a conformational instability in distant parts of the tRNA molecule.