Crystal structure of Pyrococcus horikoshii tryptophanyl-tRNA synthetase and structure-based phylogenetic analysis suggest an archaeal origin of tryptophanyl-tRNA synthetase

	Crystal structure of Pyrococcus horikoshii tryptophanyl-tRNA synthetase and structure-based phylogenetic analysis suggest an archaeal origin of tryptophanyl-tRNA synthetase
	Dong, XC; Zhou, MY; Zhong, C; Yang, B; Shen, N; Ding, JP
刊名	NUCLEIC ACIDS RESEARCH
	2010
卷号	38 期号:4 页码:1401-1412
通讯作者	Ding, JP (reprint author), Chinese Acad Sci, State Key Lab Mol Biol, Shanghai 200031, Peoples R China.,jpding@sibs.ac.cn
英文摘要	The ancient and ubiquitous aminoacyl-tRNA synthetases constitute a valuable model system for studying early evolutionary events. So far, the evolutionary relationship of tryptophanyl- and tyrosyl-tRNA synthetase (TrpRS and TyrRS) remains controversial. As TrpRS and TyrRS share low sequence homology but high structural similarity, a structure-based method would be advantageous for phylogenetic analysis of the enzymes. Here, we present the first crystal structure of an archaeal TrpRS, the structure of Pyrococcus horikoshii TrpRS (pTrpRS) in complex with tryptophanyl-5' AMP (TrpAMP) at 3.0 A resolution which demonstrates more similarities to its eukaryotic counterparts. With the pTrpRS structure, we perform a more complete structure-based phylogenetic study of TrpRS and TyrRS, which for the first time includes representatives from all three domains of life. Individually, each enzyme shows a similar evolutionary profile as observed in the sequence-based phylogenetic studies. However, TyrRSs from Archaea/Eucarya cluster with TrpRSs rather than their bacterial counterparts, and the root of TrpRS locates in the archaeal branch of TyrRS, indicating the archaeal origin of TrpRS. Moreover, the short distance between TrpRS and archaeal TyrRS and that between bacterial and archaeal TrpRS, together with the wide distribution of TrpRS, suggest that the emergence of TrpRS and subsequent acquisition by Bacteria occurred at early stages of evolution.
学科主题	Biochemistry & Molecular Biology
类目[WOS]	Biochemistry & Molecular Biology
关键词[WOS]	AMINO-ACID ACTIVATION ; GENETIC-CODE ; SEQUENCE ALIGNMENTS ; ACTIVE-SITE ; EVOLUTION ; BINDING ; ANGIOGENESIS ; RECOGNITION ; DIVERGENCE ; COMPONENTS
收录类别	SCI
语种	英语
WOS记录号	WOS:000275270500038
内容类型	期刊论文
版本	出版稿
源URL	[http://202.127.25.143/handle/331003/996]
专题	上海生化细胞研究所_上海生科院生化细胞研究所
推荐引用方式 GB/T 7714	Dong, XC,Zhou, MY,Zhong, C,et al. Crystal structure of Pyrococcus horikoshii tryptophanyl-tRNA synthetase and structure-based phylogenetic analysis suggest an archaeal origin of tryptophanyl-tRNA synthetase[J]. NUCLEIC ACIDS RESEARCH,2010,38(4):1401-1412.
APA	Dong, XC,Zhou, MY,Zhong, C,Yang, B,Shen, N,&Ding, JP.(2010).Crystal structure of Pyrococcus horikoshii tryptophanyl-tRNA synthetase and structure-based phylogenetic analysis suggest an archaeal origin of tryptophanyl-tRNA synthetase.NUCLEIC ACIDS RESEARCH,38(4),1401-1412.
MLA	Dong, XC,et al."Crystal structure of Pyrococcus horikoshii tryptophanyl-tRNA synthetase and structure-based phylogenetic analysis suggest an archaeal origin of tryptophanyl-tRNA synthetase".NUCLEIC ACIDS RESEARCH 38.4(2010):1401-1412.