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Gene Review:

thrS - threonyl-tRNA synthetase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK1717, JW1709

Sankaranarayanan, R. et al., Kim, C.W. et al., Plumbridge, J.A. et al., Mayaux, J.F. et al., Plumbridge, J.A. et al.

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Disease relevance of thrS

The nucleotide sequence of thrS, the gene encoding dimeric Escherichia coli threonyl-tRNA synthetase [L-threonine:tRNAThr ligase (AMP forming), 6.1.1.3], has been determined [1].

High impact information on thrS

In order to investigate the basis of amino acid recognition and to understand the role played by the zinc ion present in the active site of threonyl-tRNA synthetase, we have determined the crystal structures of complexes of an active truncated form of the enzyme with a threonyl adenylate analog or threonine [2].
Here, we show that the N-terminal domains of three E. coli multidomain proteins such as lysyl-tRNA synthetase, threonyl-tRNA synthetase, and aconitase are potent solubility enhancers for various C-terminal heterologous proteins [3].
Although the steady-state levels of threonyl-tRNA synthetase and phenylalanyl-tRNA synthetase produced by the presence of the plasmid differed by a factor of 10, their pulse-labeled mRNA levels were about the same [4].
Plasmid pB1 carries the genes for threonyl-tRNA synthetase, phenylalanyl-tRNA synthetase, and translation initiation factor IF3 [5].

References

Structural and transcriptional evidence for related thrS and infC expression. Mayaux, J.F., Fayat, G., Fromant, M., Springer, M., Grunberg-Manago, M., Blanquet, S. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase. Sankaranarayanan, R., Dock-Bregeon, A.C., Rees, B., Bovee, M., Caillet, J., Romby, P., Francklyn, C.S., Moras, D. Nat. Struct. Biol. (2000) [Pubmed]
N-terminal domains of native multidomain proteins have the potential to assist de novo folding of their downstream domains in vivo by acting as solubility enhancers. Kim, C.W., Han, K.S., Ryu, K.S., Kim, B.H., Kim, K.H., Choi, S.I., Seong, B.L. Protein Sci. (2007) [Pubmed]
Escherichia coli phenylalanyl-tRNA synthetase operon: transcription studies of wild-type and mutated operons on multicopy plasmids. Plumbridge, J.A., Springer, M. J. Bacteriol. (1982) [Pubmed]
Escherichia coli phenylalanyl-tRNA synthetase operon: characterization of mutations isolated on multicopy plasmids. Plumbridge, J.A., Springer, M. J. Bacteriol. (1982) [Pubmed]

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