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Soman, Smitha, Ram, Siya. (1402). Arginine to glutamine mutation in the substrate binding region impaired the isopentenyl activity of Mycobacterium tuberculosis MiaA. , 13(1), 3-9. doi: 10.22099/mbrc.2023.47247.1825
Smitha Soman; Siya Ram. "Arginine to glutamine mutation in the substrate binding region impaired the isopentenyl activity of Mycobacterium tuberculosis MiaA". , 13, 1, 1402, 3-9. doi: 10.22099/mbrc.2023.47247.1825
Soman, Smitha, Ram, Siya. (1402). 'Arginine to glutamine mutation in the substrate binding region impaired the isopentenyl activity of Mycobacterium tuberculosis MiaA', , 13(1), pp. 3-9. doi: 10.22099/mbrc.2023.47247.1825
Soman, Smitha, Ram, Siya. Arginine to glutamine mutation in the substrate binding region impaired the isopentenyl activity of Mycobacterium tuberculosis MiaA. , 1402; 13(1): 3-9. doi: 10.22099/mbrc.2023.47247.1825

Arginine to glutamine mutation in the substrate binding region impaired the isopentenyl activity of Mycobacterium tuberculosis MiaA

Molecular Biology Research Communications
دوره 13، شماره 1، 2024، صفحه 3-9    اصل مقاله (186.06 K)
نوع مقاله: Original article
شناسه دیجیتال (DOI): 10.22099/mbrc.2023.47247.1825
نویسندگان
Smitha Soman* 1؛ Siya Ram1، 2
1School of Biotechnology, Gautam Buddha University, Gautam Budh Nagar, Greater Noida, Uttar Pradesh, India
2School of Sciences, Indira Gandhi National Open University, Maidan Garhi, New Delhi, India
چکیده
tRNAs act as adaptors during protein synthesis and are chemically modified post-transcriptionally for their structural stability as well as accuracy of the translation. Hypomodifications of tRNAs are known to cause various human diseases, including cancer. Studies in bacteria and yeasts showed that levels of tRNA modifications vary under different stress conditions, enabling the organism to modulate gene expression for survival. Isopentelylation of the base 37 (i6A37) in the anticodon stem-loop by tRNA isopentenyltransferase (MiaA) is well-conserved modification present in prokaryotes and eukaryotes. i6A37 modification increases both the speed and fidelity of translation. A homozygous p.Arg323Gln mutation in the tRNA binding region of tRNA isopentenyltransferase reduced i6A37 levels in humans, affecting mitochondrial translation and thereby causing neurodevelopmental disorder. In this study, we mutated the Arg residue at the conserved position to Gln in Mycobacterium tuberculosis (M. tb) MiaA and analyzed the i6A modification activity of the enzyme on its target tRNAs. We found that p.Arg274Gln mutant MiaA could not modify the target tRNAs, tRNALeuCAA, tRNAPheGAA, and tRNASerCGA from M. tb, confirming the role of Arg residue in tRNA binding.
کلیدواژه‌ها
MiaA؛ DMAPP؛ SDM؛ M. tuberculosis؛ i6A؛ isopentenylation
مراجع
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