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Abstract

Methylation is a chemical modification that occurs in all life forms and is crucial for a wide variety of essential cellular processes, occurring on proteins, nucleic acids, lipids, and small molecules. The identification and characterization of novel methyltransferases leads to a clearer understanding of biological processes affected by the reactions they catalyze. The yeast gene YKL162C encodes for a protein that currently has no demonstrated activity, but two studies have shown its localization in mitochondria. The predicted human homolog of Ykl162cp is NADH:Ubiquinone Oxidoreductase Complex Assembly Factor 7 (NDUFAF7). This protein is an assembly factor that promotes protein-protein interactions between specific subunits of Complex I (CI) within the inner mitochondrial membrane. Complex I is involved in several physiological activities in the cell, some of which include metabolite transport and ATP synthesis. Yeast is an excellent model organism to study mitochondrial diseases due to the high degree of similarity between yeast and human mitochondria. There are a wide variety of mitochondrial diseases associated with Complex I dysregulation. It is important to note that Saccharomyces cerevisiae does not contain Complex I, which suggests Ykl162cp may have a different function in yeast. In contrast, Saccharomyces cerevisiae yeast contains NADH dehydrogenases Ndi1, Nde1, and Nde2, to serve similar functions to Complex I. Being able to use model organisms, such as yeast, to help understand the basic biological and chemical mechanisms behind mitochondrial function and expand our understanding of processes that arginine methylation can regulate.