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嗜热栖热菌HB 27中tRNA与tRNA(鸟苷-2')甲基转移酶的识别机制

Recognition mechanism of tRNA with tRNA(guanosine-2')methyltransferase from Thermus thermophilus HB 27.

作者信息

Matsumoto T, Watanabe K, Ohta T

出版信息

Nucleic Acids Symp Ser. 1984(15):131-4.

PMID:6522282
Abstract

rRNA(Gm)methyltransferase from an extreme thermophile, Thermus thermophilus HB 27 specifically methylates the 2'-OH of the ribose ring of G18 in the invariant G18-G19 sequence in the D loop of tRNA. The interaction site on tRNA was presumed to be the D loop and stem structure. Destruction of tertiary structure of tRNA caused by heat resulted in a great decrease in the acceptor activity of methyl group. It was suggested by CD measurement that a conformational change of tRNA occurs when it forms an equimolar complex with Gm-methylase.

摘要

来自嗜热栖热菌HB 27的rRNA(Gm)甲基转移酶特异性地使tRNA D环中不变的G18 - G19序列中G18核糖环的2'-OH甲基化。tRNA上的相互作用位点被推测为D环和茎结构。热导致的tRNA三级结构破坏导致甲基受体活性大幅下降。圆二色测量表明,当tRNA与Gm甲基化酶形成等摩尔复合物时会发生构象变化。

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