In silico Analysis of Ribosome-Inactivating Protein (Tritin) from Common Wheat Plants (Triticum aestivum L.)

Abstract

Ribosome-inactivating proteins (RIPs) are one of the enzymes that inhibit protein synthesis after depurination of a specific adenine in ribosomal RNA. The tritin is one of type I RIPs that include RNA-N glycosidase domain from RIP family. In the present study, cDNA encoding tritin from leaves of wheat Kutluk-94 cultivar was isolated and cloned into pGEM-T Easy vector. The recombinant plasmid was sequenced. The different bioinformatics tools were used for assessment of tritin protein characteristics. A total of 38 tritin-like sequences were identified in some monocot plants. Results showed that tritin protein have conserved domain (Ricin-A) found in other RIPs associated with RNA N-glycosidase activity and shows chancing homology to the RIPs in other plant species. According to multiple sequence alignment, tritin has conserved amino acids which are crucial role in RNA N-glycosidase activity. Our study illustrates that results obtained from in silico analyses could provide a perspective to another researcher about molecular and structural properties of tritin protein.