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LC‐MS assay targeting the mycobacterial indirect aminoacylation pathway uncovers glutaminase activities of the nondiscriminating aspartyl‐synthetase by Chew, Bing Liang Alvin; Tanoto, Frederick Reinhart; Luo, Dahai is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is LC‐MS assay targeting the mycobacterial indirect aminoacylation pathway uncovers glutaminase activities of the nondiscriminating aspartyl‐synthetase about?

The synthesis of asparagine (Asn)‐tRNA^Asn^ in most prokaryotes uses an indirect aminoacylation pathway involving a nondiscriminating aspartyl synthetase (ND‐AspRS) and a glutamine amidotransferase (GatCAB). This was recently implicated as an adaptive mistranslation mechanism for antimicrobial resistance in Mycobacterium tuberculosis, but it remains poorly understood. We report an accessible liquid chromatography–mass spectrometry method with unparalleled chemical specificity, sensitivity, and quantification over the current assays to enable the direct analysis and drug screening campaigns of this pathway. Through this method, we show that the mycobacterial ND‐AspRS stimulates the glutaminase activity of GatCAB. We further uncover novel glutaminase activity of the synthetase. These biological insights help better understand the indirect aminoacylation biology and allude to new roles beyond protein translation.

Who reads LC‐MS assay targeting the mycobacterial indirect aminoacylation pathway uncovers glutaminase activities of the nondiscriminating aspartyl‐synthetase?

Author

Chew, Bing Liang Alvin; Tanoto, Frederick Reinhart; Luo, Dahai

Publisher

Elsevier Science; Wiley (John Wiley & Sons); Wiley-Blackwell; Wiley (ISSN 0014-5793)

Published

2020

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)