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Duplication of leucyl-tRNA synthetase in an archaeal extremophile may play a role in adaptation to variable environmental conditions.
Journal of Biological Chemistry ( IF 5.5 ) Pub Date : 2020-04-03 , DOI: 10.1074/jbc.ra118.006481
Christopher S Weitzel 1 , Li Li 2, 3 , Changyi Zhang 4, 5 , Kristen K Eilts 6 , Nicholas M Bretz 6 , Alex L Gatten 2 , Rachel J Whitaker 4, 5 , Susan A Martinis 2, 3
Affiliation  

Aminoacyl-tRNA synthetases (aaRSs) are ancient enzymes that play a fundamental role in protein synthesis. They catalyze the esterification of specific amino acids to the 3'-end of their cognate tRNAs and therefore play a pivotal role in protein synthesis. Although previous studies suggest that aaRS-dependent errors in protein synthesis can be beneficial to some microbial species, evidence that reduced aaRS fidelity can be adaptive is limited. Using bioinformatics analyses, we identified two distinct leucyl-tRNA synthetase (LeuRS) genes within all genomes of the archaeal family Sulfolobaceae. Remarkably, one copy, designated LeuRS-I, had key amino acid substitutions within its editing domain that would be expected to disrupt hydrolytic editing of mischarged tRNALeu and to result in variation within the proteome of these extremophiles. We found that another copy, LeuRS-F, contains canonical active sites for aminoacylation and editing. Biochemical and genetic analyses of the paralogs within Sulfolobus islandicus supported the hypothesis that LeuRS-F, but not LeuRS-I, functions as an essential tRNA synthetase that accurately charges leucine to tRNALeu for protein translation. Although LeuRS-I was not essential, its expression clearly supported optimal S. islandicus growth. We conclude that LeuRS-I may have evolved to confer a selective advantage under the extreme and fluctuating environmental conditions characteristic of the volcanic hot springs in which these archaeal extremophiles reside.

中文翻译:

在古细菌极端微生物中,亮氨酰-tRNA合成酶的复制可能在适应可变的环境条件中起作用。

氨酰基-tRNA合成酶(aaRSs)是古老的酶,在蛋白质合成中起基本作用。它们催化特定氨基酸酯化至同源tRNA的3'端,因此在蛋白质合成中起关键作用。尽管以前的研究表明蛋白质合成中依赖aaRS的错误可能对某些微生物有益,但减少aaRS保真度可以适应的证据有限。使用生物信息学分析,我们在古菌科硫磺科的所有基因组中鉴定了两个不同的亮氨酰-tRNA合成酶(LeuRS)基因。值得注意的是,一个名为LeuRS-1的拷贝在其编辑域内具有关键的氨基酸取代,这有望破坏带错电荷的tRNALeu的水解编辑,并导致这些极端微生物的蛋白质组内发生变化。我们发现另一个副本LeuRS-F包含用于氨基酰化和编辑的规范活性位点。对岛S属植物内旁系同源物的生化和遗传分析支持以下假说,即LeuRS-F而非LeuRS-1充当一种必需的tRNA合成酶,可将亮氨酸准确地带入tRNALeu进行蛋白质翻译。尽管LeuRS-1不是必需的,但其表达显然支持了最佳的岛状链球菌生长。我们得出的结论是,LeuRS-1可能已经进化为在这些古生极端微生物所居住的火山温泉所处的极端和多变的环境条件下赋予选择优势。对岛S属植物内旁系同源物的生化和遗传分析支持以下假说,即LeuRS-F而非LeuRS-1充当一种必需的tRNA合成酶,可将亮氨酸准确地带入tRNALeu进行蛋白质翻译。尽管LeuRS-1不是必需的,但其表达显然支持了最佳的岛状链球菌生长。我们得出的结论是,LeuRS-1可能已经进化为在这些古生极端微生物所居住的火山温泉所处的极端和多变的环境条件下赋予选择优势。对岛S属植物内旁系同源物的生化和遗传分析支持以下假说,即LeuRS-F而非LeuRS-1充当一种必需的tRNA合成酶,可将亮氨酸准确地带入tRNALeu进行蛋白质翻译。尽管LeuRS-1不是必需的,但其表达显然支持了最佳的岛状链球菌生长。我们得出的结论是,LeuRS-1可能已经进化为在这些古生极端微生物所居住的火山温泉所处的极端和多变的环境条件下赋予选择优势。
更新日期:2020-04-03
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