Nick Davis

TL;DR: In this article, the authors proposed a pathophysiological link between ITP and chronic Helicobacter pylori infection, which is typically a diagnosis of exclusion, assigned by clinicians after ruling out other identifiable etiologies.

TL;DR: It is shown that modification of uridine at anticodon position 34 (U34) by the tRNA-modifying enzymes Elp1, Elp3, Sml3 and Trm9 is critical for proteostasis, and that stress response proteins whose genes are enriched in codons decoded by tRNAs are overrepresented in protein aggregates of the ELP1, SLM3 and TRM9 KO strains.

TL;DR: Proteomic analysis of the t6A-deficient strain (sua5 mutant) revealed a global mistranslation leading to protein aggregation without regard to physicochemical properties or t 6A-dependent or biased codon usage in parent genes, but loss of sua5 led to increased expression of soluble proteins for mitochondrial function, protein quality processing/trafficking, oxidative stress response, and energy homeostasis.

TL;DR: Downstream analysis of the transcriptomic data suggested that the absence of Q triggers an atypical oxidative stress response, confirmed by the detection of slightly elevated reactive oxygen species (ROS) levels in the mutant, increased sensitivity to hydrogen peroxide and paraquat, and a subtle growth phenotype in a strain prone to accumulation of ROS.