Genetic Diversity and its Impact on Post Translational Modifications of PKC and bml-Beta Tubulin Homolog Proteins in Different Species and Strains of Sordaria

Abstract

Protein Kinase C (PKC) and tubulin homologs are present in all eukaryotes and play significant role in growth, development and cell differentiation through phosphorylation and de-phosphorylation of other proteins. In this study, we have amplified PKC and beta tubulin homolog bml gene from six strains and F3 and F4 generations of Sordaria fimicola collected from the Evolution Canyon-1. Sequenced products of 464 bp of tubulin gene and 548 bp for PKC gene were aligned to observe the genetic variations between the eight parental strains of S. fimicola and reference sequence of S. fimicola. Total six polymorphic sites were observed in case of tubulin gene out of which 5 sites were common among strains isolated from the s-slope of Evolution Canyon (EC). Genetic variations in four nucleotides were observed for PKC gene i.e. C (150) T; C (186) A; C (429) G and T (521) A which were common for S1, S2 and S3 strains, while point mutation C (497) G was detected only in S2 and S3 strains. Post translational modifications (PTMs) of both proteins were predicted and compared with the reference sequences of Neurospora crassa and Sordaria macrospora by using different PTMs predictor servers. Phosphorylation and glycosylation in different species of Sordaria as well as N. crassa was calculated on Serine (S), Tyrosine (Y) and Threonine (T) residues by NetPhos and YinOYang.