Leucyl-tRNA synthetase from the ancestral bacterium Aquifex aeolicus contains relics of synthetase evolution.

Content Provider	Semantic Scholar
Author	Zhao, Ming-Wei Xu, Minrong Eriani, Gilbert Wang, En-Duo
Copyright Year	2005
Abstract	The editing reactions catalyzed by aminoacyl-tRNA synthetases are critical for the faithful protein synthesis by correcting misactivated amino acids and misaminoacylated tRNAs. We report that the isolated editing domain of leucyl-tRNA synthetase from the deep-rooted bacterium Aquifex aeolicus (alphabeta-LeuRS) catalyzes the hydrolytic editing of both mischarged tRNA(Leu) and minihelix(Leu). Within the domain, we have identified a crucial 20-amino-acid peptide that confers editing capacity when transplanted into the inactive Escherichia coli LeuRS editing domain. Likewise, fusion of the beta-subunit of alphabeta-LeuRS to the E. coli editing domain activates its editing function. These results suggest that alphabeta-LeuRS still carries the basic features from a primitive synthetase molecule. It has a remarkable capacity to transfer autonomous active modules, which is consistent with the idea that modern synthetases arose after exchange of small idiosyncratic domains. It also has a unique alphabeta-heterodimeric structure with separated catalytic and tRNA-binding sites. Such an organization supports the tRNA/synthetase coevolution theory that predicts sequential addition of tRNA and synthetase domains.
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://emboj.embopress.org/content/embojnl/24/7/1430.full.pdf
Alternate Webpage(s)	http://www.sibcb.ac.cn/publications/2005/2005-TheEMBOJournal24-1430.pdf
PubMed reference number	15775966v1
Volume Number	24
Issue Number	7
Journal	The EMBO journal
Language	English
Access Restriction	Open
Subject Keyword	Amino Acids Amino Acyl-tRNA Synthetases Binding Sites Inactive - Biochemical Activity Level Leucine-Specific tRNA Ligase Protein Biosynthesis Transfer RNA Aminoacylation
Content Type	Text
Resource Type	Article