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Gene Review:

asnS - asparaginyl tRNA synthetase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK0921, JW0913, lcs, tss

Madern, D. et al., Iwasaki, W. et al., Roy, H. et al., Archontis, G. et al., Aoki, H. et al., et al.

Archontis, Simonson, Karplus,

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Disease relevance of asnS

Its position on the E. coli chromosome was determined at 20.8 min between the asnS and pepN loci [1].

High impact information on asnS

Analysis of the completed archaeal genomes reveals that all archaea that possess asparaginyl-tRNA synthetase (AsnRS) also display a second ORF encoding an AsnRS truncated from its anticodon binding-domain (AsnRS2) [2].
Structural basis of the water-assisted asparagine recognition by asparaginyl-tRNA synthetase [3].
Asparaginyl-tRNA synthetase (AsnRS) is a member of the class-II aminoacyl-tRNA synthetases, and is responsible for catalyzing the specific aminoacylation of tRNA(Asn) with asparagine [3].
A conserved active site lysine (Lys198 in Escherichia coli) that recognizes the Asp side-chain is changed to a leucine residue, found at the corresponding position in asparaginyl-tRNA synthetase [4].
Asparaginyl-tRNA synthetase from Escherichia coli has significant sequence homologies with yeast aspartyl-tRNA synthetase [5].

Chemical compound and disease context of asnS

Asparaginyl-tRNA synthetase from the Escherichia coli temperature-sensitive strain HO202. A proline replacement in motif 2 is responsible for a large increase in Km for asparagine and ATP [6].

Biological context of asnS

Analysis of the DNA sequence and the correspondence to that of the partial protein sequence has identified the complementing factor as asparaginyl-tRNA synthetase [7].

Analytical, diagnostic and therapeutic context of asnS

The Escherichia coli K12 mutant gene, asnS40, coding for asparaginyl-tRNA synthetase (AsnRS) in the temperature-sensitive strain HO202, was isolated from genomic DNA using the Polymerase Chain Reaction [6].

References

Variation of cofactor levels in Escherichia coli. Sequence analysis and expression of the pncB gene encoding nicotinic acid phosphoribosyltransferase. Wubbolts, M.G., Terpstra, P., van Beilen, J.B., Kingma, J., Meesters, H.A., Witholt, B. J. Biol. Chem. (1990) [Pubmed]
When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism. Roy, H., Becker, H.D., Reinbolt, J., Kern, D. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
Structural basis of the water-assisted asparagine recognition by asparaginyl-tRNA synthetase. Iwasaki, W., Sekine, S., Kuroishi, C., Kuramitsu, S., Shirouzu, M., Yokoyama, S. J. Mol. Biol. (2006) [Pubmed]
Binding free energies and free energy components from molecular dynamics and Poisson-Boltzmann calculations. Application to amino acid recognition by aspartyl-tRNA synthetase. Archontis, G., Simonson, T., Karplus, M. J. Mol. Biol. (2001) [Pubmed]
Asparaginyl-tRNA synthetase from Escherichia coli has significant sequence homologies with yeast aspartyl-tRNA synthetase. Anselme, J., Härtlein, M. Gene (1989) [Pubmed]
Asparaginyl-tRNA synthetase from the Escherichia coli temperature-sensitive strain HO202. A proline replacement in motif 2 is responsible for a large increase in Km for asparagine and ATP. Madern, D., Anselme, J., Härtlein, M. FEBS Lett. (1992) [Pubmed]
The asparaginyl-tRNA synthetase gene encodes one of the complementing factors for thermosensitive translation in the Escherichia coli mutant strain, N4316. Aoki, H., Yaworsky, P.J., Patel, S.D., Margolin-Brzezinski, D., Park, K.S., Ganoza, M.C. Eur. J. Biochem. (1992) [Pubmed]

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