key: cord-1050131-ef8cuyc2 authors: Zhang, Fangliang title: Editorial: Waken the Silent Majority: Principles and Pathogenic Significance of Non-Acetyl Acylation and Other Understudied Post-Translational Modifications date: 2022-04-13 journal: Front Cell Dev Biol DOI: 10.3389/fcell.2022.896324 sha: 3eb6585902dada1c2fbc82e2e18b251da4cb01a2 doc_id: 1050131 cord_uid: ef8cuyc2 nan conditions. Finally, new clues for interpreting the role of the arginylation enzyme ATE1 was provided in the original research "Regulation of Mitochondrial Respiratory Chain Complex Levels, Organization, and Function by Arginyltransferase 1" by Jiang et al. (contributed by my own research group). In this study, a small fraction of ATE1 was found located inside mitochondria and is essential for the proper function of mitochondria in respiration. Intriguingly, homologues of eukaryotic ATE1 can be traced back to alpha-proteobacteria, relatives of the ancient ancestor of mitochondria. This connection between ATE1 and mitochondria may constitute a new angle for understanding the diverse functions of ATE1 in cellular metabolism (Brower and Varshavsky, 2009; Zhang et al., 2015) , stress response (Wiley et al., 2020; Kumar et al., 2016; Deka et al., 2016) , and oxygen sensing (Moorthy et al., 2022) . Overall, while arginylation is still a poorly understood process, the papers presented in this Research Topic will help to shorten the gap. Hopefully with more research and further advancements of techniques including proteomic study tools, a more comprehensive picture of arginylation will soon be on the horizon. FZ wrote this manuscript. Cloning and Functional Analysis of the Arginyl-tRNA-Protein Transferase Gene ATE1 of Saccharomyces cerevisiae Ablation of Arginylation in the Mouse N-End Rule Pathway: Loss of Fat, Higher Metabolic Rate, Damaged Spermatogenesis, and Neurological Perturbations Protein Arginylation Regulates Cellular Stress Response by Stabilizing HSP70 and HSP40 Transcripts Aminoacyl-transferases and the N-End Rule Pathway of Prokaryotic/ eukaryotic Specificity in a Human Pathogen The N-End Rule Pathway Controls Multiple Functions during Arabidopsis Shoot and Leaf Development A Soluble Amino Acid-Incorporating System from Rat Liver Soluble Amino Acid Incorporating System from Rat Liver Complete Purification of arginyl-tRNA: Protein Arginyltransferase from Hog Kidney and Production of its Antibody Posttranslational Arginylation Enzyme Ate1 Affects DNA Mutagenesis by Regulating Stress Response Oxygen Sensing in Plants Is Mediated by an N-End Rule Pathway for Protein Destabilization The Evolutionarily Conserved Arginyltransferase 1 Mediates a pVHLindependent Oxygen-Sensing Pathway in Mammalian Cells ATE1-Mediated Post-Translational Arginylation Is an Essential Regulator of Eukaryotic Cellular Homeostasis Posttranslational Arginylation Enzyme Arginyltransferase1 Shows Genetic Interactions with Specific Cellular Pathways In Vivo Arginylation Regulates Purine Nucleotide Biosynthesis by Enhancing the Activity of Phosphoribosyl Pyrophosphate Synthase The author declares that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.