Genetic and Post-Translational Modification Analysis of Translational Associated Protein RKM4 in Sordaria fimicola

Ribosomal-lysine N-methyltransferases are involved in important biological processes and methylate specific lysine residues of different subunits of the translational machinery. The current study investigates natural genetic variations and posttranslational modifications in the RKM4 gene in six parental strains of Sordaria fimicola. For this purpose, DNA was extracted and RKM4 regions of all strains of S. fimicola were amplified by TD-PCR (touchdown PCR) conditions. Polymorphisms are observed on twelve different sites in the RK-MTases genes and six non-synonymous substitutions are found. Different bioinformatics tools were used to predict the post-translational modifications after translating the DNA sequence into the protein sequence by EMBOSS Transeq. The current study reports 28 phosphorylation sites for the S-1, S-2, N-5 strains, 26 sites for the S-3, N-6 strains and 27 sites for the N-7 strain. Seven potential lysine acetylation sites for the S-1, S-2, S-3 and five lysine acetylation sites for the N-5, N-6 and N-7 strains of S. fimicola are identified. Methylation at arginine and lysine residues is predicted using the PMes server. Only arginine residues exhibit methylation for RKM4 protein methyltransferase, which includes a total of one and six arginine methylation sites for S. fimicola and Saccharomyces cerevisiae, respectively. In conclusion, the present study indicates that protein methyltransferases are meant for methylation of lysine residues and they undergo diverse types of post-translational modifications in filamentous fungi. (C) 2020 Friends Science Publishers