Redox status affects the catalytic activity of glutamyl-tRNA synthetase
Author
dc.contributor.author
Katz, Assaf
Author
dc.contributor.author
Banerjee, Rajat
Author
dc.contributor.author
de Armas, Merly
Author
dc.contributor.author
Ibba, Michael
Author
dc.contributor.author
Orellana, Omar
Admission date
dc.date.accessioned
2018-12-20T14:12:44Z
Available date
dc.date.available
2018-12-20T14:12:44Z
Publication date
dc.date.issued
2010
Cita de ítem
dc.identifier.citation
Biochemical and Biophysical Research Communications, Volumen 398, Issue 1, 2018, Pages 51-55
Identifier
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10902104
Identifier
dc.identifier.issn
0006291X
Identifier
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10.1016/j.bbrc.2010.06.031
Identifier
dc.identifier.uri
https://repositorio.uchile.cl/handle/2250/154785
Abstract
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Glutamyl-tRNA synthetases (GluRS) provide Glu-tRNA for different processes including protein synthesis, glutamine transamidation and tetrapyrrole biosynthesis. Many organisms contain multiple GluRSs, but whether these duplications solely broaden tRNA specificity or also play additional roles in tetrapyrrole biosynthesis is not known. Previous studies have shown that GluRS1, one of two GluRSs from the extremophile Acidithiobacillus ferrooxidans, is inactivated when intracellular heme is elevated suggesting a specific role for GluRS1 in the regulation of tetrapyrrole biosynthesis. We now show that, in vitro, GluRS1 activity is reversibly inactivated upon oxidation by hemin and hydrogen peroxide. The targets for oxidation-based inhibition were found to be cysteines from a SWIM zinc-binding motif located in the tRNA acceptor helix-binding domain. tRNAGlu was able to protect GluRS1 against oxidative inactivation by hemin plus hydrogen peroxide. The sensitivity to oxidation of A. ferrooxidan