Publications
2005
Zhao M W, Zhu B, Hao R, Xu M G, Eriani G, Wang E D
Leucyl-tRNA synthetase from the ancestral bacterium Aquifex aeolicus contains relics of synthetase evolution Journal Article
In: EMBO J, vol. 24, no. 7, pp. 1430-1439, 2005, ISBN: 15775966, (0261-4189 (Print) Journal Article).
Abstract | Links | BibTeX | Tags: Amino Acid Sequence Bacteria/*genetics Comparative Study Escherichia coli/genetics *Evolution, ERIANI, Molecular Leucine-tRNA Ligase/*genetics/*metabolism Models, Molecular Molecular Sequence Data Protein Biosynthesis/*genetics Protein Structure, Non-U.S. Gov't Sequence Alignment, Tertiary/genetics Research Support, Unité ARN
@article{,
title = {Leucyl-tRNA synthetase from the ancestral bacterium Aquifex aeolicus contains relics of synthetase evolution},
author = {M W Zhao and B Zhu and R Hao and M G Xu and G Eriani and E D Wang},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15775966},
isbn = {15775966},
year = {2005},
date = {2005-01-01},
journal = {EMBO J},
volume = {24},
number = {7},
pages = {1430-1439},
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.},
note = {0261-4189 (Print)
Journal Article},
keywords = {Amino Acid Sequence Bacteria/*genetics Comparative Study Escherichia coli/genetics *Evolution, ERIANI, Molecular Leucine-tRNA Ligase/*genetics/*metabolism Models, Molecular Molecular Sequence Data Protein Biosynthesis/*genetics Protein Structure, Non-U.S. Gov't Sequence Alignment, Tertiary/genetics Research Support, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
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.