Molecular and functional properties of an archaeal phenylalanyl-tRNA synthetase from the hyperthermophile Sulfolobus solfataricus

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology Pub Date : 2002-04-29 DOI:10.1016/S0167-4838(02)00223-6

Barbara Lombardo, Gennaro Raimo, Vincenzo Bocchini

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引用次数: 5

Abstract

An archaeal phenylalanyl-tRNA synthetase (FRS) has been purified from the hyperthermophile Sulfolobus solfataricus (Ss). This enzyme is a heterotetramer made of two different subunits whose molecular mass is 56 kDa and 64 kDa, respectively. As thought, SsFRS is essential for the in vitro poly(Phe) synthesis. Interestingly, the enzyme is able to aminoacylate only endogenous tRNA but it does not seem to be a strictly ATP-dependent synthetase. SsFRS interacts with the elongation factor 1α isolated from the same source; this caused a significant enhancement of the SstRNA aminoacylation efficiency, thus indicating that, as well as in eukarya, in this archaeon a tRNA channelling mechanism should occur. The overall results presented in this paper show that the archaeal SsFRS behaves as the analogous enzymes isolated from eukaryal sources rather than those from eubacterial organisms.

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古细菌苯丙酰- trna合成酶的分子和功能特性

从嗜热菌Sulfolobus solfataricus (Ss)中纯化出一种古细菌苯丙烯酰trna合成酶(FRS)。该酶是由两个不同的亚基组成的异四聚体，其分子质量分别为56 kDa和64 kDa。综上所述，SsFRS对体外聚苯醚合成至关重要。有趣的是，这种酶只能对内源性tRNA进行氨基化，但它似乎并不是一种严格依赖atp的合成酶。SsFRS与从同一来源分离的延伸因子1α相互作用;这导致了SstRNA氨基酰化效率的显著增强，从而表明，在真核生物中，在这个古菌中应该发生tRNA通道机制。本文的总体结果表明，古细菌的SsFRS表现为从真核生物中分离出来的类似酶，而不是从真核生物中分离出来的类似酶。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

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