PJB-2020-2
In silico investigation of glycosylation of SET9 protein in different strains of Sordaria fimicola
Iqra Mobeen, Rabia Arif and Muhammad Saleem
Abstract
Glycosylation is the most abundant and complex type of post-translational modification (PTM), which diversifies the protein functions and is affected by environmental stress. This study has investigated the polymorphism and glycosylation of the SET9 (a histone methyltransferase) protein of six strains of Sordaria fimicola and Neurospora crassa for the first time. Various bioinformatics tools are used to predict the O and N-glycosylation and those sites, which were common and have the highest EVP (enhancement value product) value, are chosen. Two N-glycosylation sites Asn205, Asn262 are found conserved in the N. crassa and all strains of S. fimicola, predicted by NetNGlyc 1.0. Seven O-glycosylation sites are reported on serine and threonine residues in SFS (South-facing slope) strains, which are presented at Ser74, Ser219, Ser292, Thr330, Ser320, Thr333, and Ser412, predicted by NetOGlyc 4.0 and ISOGlyP. While the NFS (North-facing slope) strains have five O-glycosylation sites similar to the SFS strains except for Ser320, not present in NFS strains. N. crassa has four sites similar to the SFS and NFS strains with two missing sites Ser320 and Ser412. These all sites are also presented on the 3D models of the SET9 protein. PolyView-2D, NetSurfP, and I-TASSER are used to predict the 2D and 3D structures and surface accessibility of glycosylated sites of the SET9. Polymorphism reported at five sites in the SFS strains and at one site in the NFS strains of the SET9 region, which clearly shows the effects of environmental stress on the SFS strains. The functions of the glycosylated sites of SET9 in S. fimicola are not known, but this study is evidenced by the more glycosylation sites in SFS strains than NFS strains. Therefore, the current study concludes that environmental stress is responsible for polymorphism, which alters the genes expression and this leads towards the creation of more diverse types of glycoproteins through PTMs that are specifically preferred by the organisms facing environmental stress
To Cite this article:
Mobeen, I., R. Arif and M. Saleem. 2022. In silico investigation of glycosylation of SET9 protein in different strains of Sordaria fimicola. Pak. J. Bot., 54(3): DOI: http://dx.doi.org/10.30848/PJB2022-3(24)
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