Genetic analysis and post-translation modifications of 60S ribosomal protein L30 in Sordaria fimicola

Ribosomes are extremely conserved organelles whose essential composition has usually been viewed as invariant. Though, recent studies have characterized remarkable variations in the expression of some ribosomal proteins (RPs) through species and very much particular effects on translation of individual mRNAs. So far, no genetic diversity and prediction of post translation modifications (PTMs) in large ribosomal subunit L30 (RpL30) protein were investigated in S. fimicola in any region of the world. To bridge this gap during the current work an attempt was made to predict post translational modifications on RpL30 protein. During the current study we used S. macrospora and Neurospora crassa as reference organisms Of the 329 nucleotide, polymorphism was observed on five nucleotide positions. The O-glycosylation was predicted on serine and threonine while glycosylation on S6 and S8 residues was found to be conserved among S. fimicola, S. macrospora and N. crassa. Altogether, total 14 sites (8Ser/4Thr/2Y) of phosphorylation modifications were observed in N. crassa and S. fimicola while S. macrospora exhibited two additional modifications i.e., Ser66 and Ser91.