Document Detail


Two complementary enzymes for threonylation of tRNA in crenarchaeota: crystal structure of Aeropyrum pernix threonyl-tRNA synthetase lacking a cis-editing domain.
MedLine Citation:
PMID:  19761773     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In protein synthesis, threonyl-tRNA synthetase (ThrRS) must recognize threonine (Thr) from the 20 kinds of amino acids and the cognate tRNA(Thr) from different tRNAs in order to generate Thr-tRNA(Thr). In general, an organism possesses one kind of gene corresponding to ThrRS. However, it has been recently found that some organisms have two different genes for ThrRS in the genome, suggesting that their proteins ThrRS-1 and ThrRS-2 function separately and complement each other in the threonylation of tRNA(Thr), one for catalysis and the other for trans-editing of misacylated Ser-tRNA(Thr). In order to clarify their three-dimensional structures, we performed X-ray analyses of two putatively assigned ThrRSs from Aeropyrum pernix (ApThrRS-1 and ApThrRS-2). These proteins were overexpressed in Escherichia coli, purified, and crystallized. The crystal structure of ApThrRS-1 has been successfully determined at 2.3 A resolution. ApThrRS-1 is a dimeric enzyme composed of two identical subunits, each containing two domains for the catalytic reaction and for anticodon binding. The essential editing domain is completely missing as expected. These structural features reveal that ThrRS-1 catalyzes only the aminoacylation of the cognate tRNA, suggesting the necessity of the second enzyme ThrRS-2 for trans-editing. Since the N-terminal sequence of ApThrRS-2 is similar to the sequence of the editing domain of ThrRS from Pyrococcus abyssi, ApThrRS-2 has been expected to catalyze deaminoacylation of a misacylated serine moiety at the CCA terminus.
Authors:
Satoru Shimizu; Ella Czarina Magat Juan; Yoshiteru Sato; Yu-Ichiro Miyashita; Md Mominul Hoque; Kaoru Suzuki; Tsubasa Sagara; Masaru Tsunoda; Takeshi Sekiguchi; Anne-Catherine Dock-Bregeon; Dino Moras; Akio Takénaka
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-09-15
Journal Detail:
Title:  Journal of molecular biology     Volume:  394     ISSN:  1089-8638     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  2009 Nov 
Date Detail:
Created Date:  2009-11-06     Completed Date:  2009-11-12     Revised Date:  2012-08-02    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  286-96     Citation Subset:  IM    
Affiliation:
Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Nagatsuda, Midori-ku, Yokohama 226-8501, Japan.
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MeSH Terms
Descriptor/Qualifier:
Aeropyrum / enzymology,  metabolism*
Amino Acid Sequence
Crystallography, X-Ray
Molecular Sequence Data
Protein Folding
Protein Structure, Tertiary
RNA, Archaeal / metabolism*
RNA, Transfer, Amino Acyl / metabolism*
Threonine / metabolism
Threonine-tRNA Ligase / chemistry*,  genetics,  metabolism
Transfer RNA Aminoacylation*
Chemical
Reg. No./Substance:
0/RNA, Archaeal; 0/RNA, Transfer, Amino Acyl; 72-19-5/Threonine; EC 6.1.1.3/Threonine-tRNA Ligase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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