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Gene Review:

Aats-glupro - Glutamyl-prolyl-tRNA synthetase

Drosophila melanogaster

Synonyms: AATS, AATs-GluPro, Aa-tRNA-syn-glupro, Aats-glu, Bifunctional aminoacyl-tRNA synthetase, ...

Seshaiah, P. et al., Cerini, C. et al., Berthonneau, E. et al., Hiatt, V. et al., Zapata, J.M. et al., et al.

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High impact information on Aats-glupro

Ulp1 normally serves to prevent the accumulation of SUMO-conjugated forms of a number of proteins, including the aminoacyl-tRNA synthetase EPRS [1].
We characterized the expression patterns of all 20 aminoacyl-tRNA synthetases and found that of the four aminoacyl-tRNA synthetase genes expressed at elevated levels in the salivary gland primordia, WRS-85D is expressed at the highest level throughout embryogenesis [2].
As shown previously for eIF-4E, the p200 subunit was also required for the translation of endogenous mRNAs in cell-free systems from Drosophila embryos [3].
Our analysis of the extant motifs suggests a possible series of events responsible for a gene fusion that gave rise to the bifunctional glutamyl-prolyl-tRNA synthetase through recombination between genomic sequences encoding the repeated units [4].
Evolution of the aminoacyl-tRNA synthetase family and the organization of the Drosophila glutamyl-prolyl-tRNA synthetase gene. Intron/exon structure of the gene, control of expression of the two mRNAs, selective advantage of the multienzyme complex [5].

Associations of Aats-glupro with chemical compounds

The stimulatory factor is separated from inorganic pyrophosphatase activity by DEAE-cellulose chromatography and from aminoacyl-tRNA synthetase activity by trichloroacetic acid precipitation [6].

References

Drosophila Ulp1, a nuclear pore-associated SUMO protease, prevents accumulation of cytoplasmic SUMO conjugates. Smith, M., Bhaskar, V., Fernandez, J., Courey, A.J. J. Biol. Chem. (2004) [Pubmed]
WRS-85D: A tryptophanyl-tRNA synthetase expressed to high levels in the developing Drosophila salivary gland. Seshaiah, P., Andrew, D.J. Mol. Biol. Cell (1999) [Pubmed]
Purification and characterization of eukaryotic polypeptide chain initiation factor 4F from Drosophila melanogaster embryos. Zapata, J.M., Martínez, M.A., Sierra, J.M. J. Biol. Chem. (1994) [Pubmed]
A gene fusion event in the evolution of aminoacyl-tRNA synthetases. Berthonneau, E., Mirande, M. FEBS Lett. (2000) [Pubmed]
Evolution of the aminoacyl-tRNA synthetase family and the organization of the Drosophila glutamyl-prolyl-tRNA synthetase gene. Intron/exon structure of the gene, control of expression of the two mRNAs, selective advantage of the multienzyme complex. Cerini, C., Semeriva, M., Gratecos, D. Eur. J. Biochem. (1997) [Pubmed]
Stimulatory factor for tRNA aminoacylation: possible product of modifier genes in Drosophila melanogaster. Hiatt, V., Hillman, R. Biochim. Biophys. Acta (1980) [Pubmed]

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