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Altered proteome in translation initiation fidelity defective eIF5G31R mutant causes oxidative stress and DNA damage
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Altered proteome in translation initiation fidelity defective eIF5G31R mutant causes oxidative stress and DNA damage
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Altered proteome in translation initiation fidelity defective eIF5G31R mutant causes oxidative stress and DNA damage
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Journal Article
Altered proteome in translation initiation fidelity defective eIF5G31R mutant causes oxidative stress and DNA damage
2022
Overview
The recognition of the AUG start codon and selection of an open reading frame (ORF) is fundamental to protein biosynthesis. Defect in the fidelity of start codon selection adversely affect proteome and have a pleiotropic effect on cellular function. Using proteomic techniques, we identified differential protein abundance in the translation initiation fidelity defective eIF5
G31R
mutant that initiates translation using UUG codon in addition to the AUG start codon. Consistently, the eIF5
G31R
mutant altered proteome involved in protein catabolism, nucleotide biosynthesis, lipid biosynthesis, carbohydrate metabolism, oxidation–reduction pathway, autophagy and re-programs the cellular pathways. The utilization of the upstream UUG codons by the eIF5
G31R
mutation caused downregulation of uridylate kinase expression, sensitivity to hydroxyurea, and DNA damage. The eIF5
G31R
mutant cells showed lower glutathione levels, high ROS activity, and sensitivity to H
2
O
2
.
