On the evolution of the tRNA-dependent amidotransferases, GatCAB and GatDE
On the evolution of the tRNA-dependent amidotransferases, GatCAB and GatDE
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DOI：
10.1016/j.jmb.2008.01.016
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发表时间：
2008-03-28
影响因子：
5.6
通讯作者：
Soll, Dieter
中科院分区：
文献类型：
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作者：
Sheppard, Kelly;Soll, Dieter
谷氨酰-tRNA合成酶和天冬酰胺酰-tRNA合成酶分别由谷氨酰-tRNA合成酶和天冬酰胺酰-tRNA合成酶在最后一个通用共同祖先（LUCA）分裂后进化而来。在LUCA中，谷氨酰-tRNAGln和天冬酰胺酰-tRNA（Asn）可能是通过tRNA依赖性酰胺基转移酶使错电荷物质谷氨酰-tRNA（Gln）和天冬酰胺酰-tRNA（Asn）酰胺化而形成的，在大多数细菌和所有已知的古细菌中仍然如此。酰胺转移酶GatCAB在生命的两个领域都有发现，而异二聚体酰胺转移酶GatDE只在水母中发现。GatB和GatE亚基属于一个独特的蛋白质家族，包括在许多真核生物的核基因组中编码的Pet 112。GatE被认为是在现代体面线出现后从GatB演变而来的。然而，我们的系统发育分析将GatE和GatB之间的分裂置于细菌和细菌之间的系统发育分裂之前，并且Pet 112是线粒体起源的。此外，GatD似乎已经出现之前的细菌-古细菌系统发育划分。因此，虽然GatDE是一种古细菌特征蛋白，但它可能与GatCAB一起存在于LUCA中。细菌保留了两种酰胺转移酶，而细菌只出现了GatCAB。GatDE的存在有利于一种独特的古细菌tRNA（Gln），这可能会阻止古细菌中的乙酰氨基-tRNA合成酶的获得。另一方面，GatCAB并不支持一种独特的tRNA（Asn），这表明tRNA（Asn）识别并不是许多细菌中天冬酰胺酰-tRNA合成酶保留的主要障碍。(C)2008爱思唯尔有限公司保留所有权利。
Glutaminyl-tRNA synthetase and asparaginyl-tRNA synthetase evolved from glutamyl-tRNA synthetase and aspartyl-tRNA synthetase, respectively, after the split in the last universal communal ancestor (LUCA). Glutaminyl-tRNAGIn and asparaginyl-tRNA(Asn) were likely formed in LUCA by amidation of the mischarged species, glutamyl-tRNA(Gln) and aspartyl-tRNA(Asn), by tRNA-dependent amidotransferases, as is still the case in most bacteria and all known archaea. The amidotransferase GatCAB is found in both domains of life, while the heterodimeric amidotransferase GatDE is found only in Archaea. The GatB and GatE subunits belong to a unique protein family that includes Pet112 that is encoded in the nuclear genomes of numerous eukaryotes. GatE was thought to have evolved from GatB after the emergence of the modern lines of decent. Our phylogenetic analysis though places the split between GatE and GatB, prior to the phylogenetic divide between Bacteria and Archaea, and Pet112 to be of mitochondrial origin. In addition, GatD appears to have emerged prior to the bacterial-archaeal phylogenetic divide. Thus, while GatDE is an archaeal signature protein, it likely was present in LUCA together with GatCAB. Archaea retained both amidotransferases, while Bacteria emerged with only GatCAB. The presence of GatDE has favored a unique archaeal tRNA(Gln) that may be preventing the acquisition of glutaminyl-tRNA synthetase in Archaea. Archaeal GatCAB, on the other hand, has not favored a distinct tRNA(Asn), suggesting that tRNA(Asn) recognition is not a major barrier to the retention of asparaginyl-tRNA synthetase in many Archaea. (C) 2008 Elsevier Ltd. All rights reserved.