Analysis of Thaumatin-Like Proteins characteristics and structure in plants and fungi by bioinformatics approaches

Plants naturally produce several classes of defense proteins, called pathogenesis-related (PR) proteins, in response to a wide range of environmental stresses .The PR protein superfamily includes 17 subfamilies designated PR1– PR17. The PR5 proteins, known as Thaumatin like proteins (TLP), have been shown to have antifungal activity against many fungal pathogens. Though, recently they are discovered in fungi and animals as well. There are several mechanisms in which TLPsact as a defense protein like being involved in specific plasma membrane component(s) of the fungal target. In this studysome characteristics of TLPs from monocotyledons, di-cotyledons and even fungi were studied. Amino acid sequences of24 TLPs obtained in FASTA format from Uniprot database. The physicochemical properties and secondary structures ofprotein sequences obtained using ProtParam and Sopma. Alignment and prediction of common secondary structures weredone by CLC software. Phylogenetic trees were drawn by Clustal W. The resulted phylogenic tree showed that Oryza sativa subsp. Japonica out grouped which had out range of isoelectric pH and Rhizoctonia solani stand in an out-group from other fungi. Random coil and then extended strand had more percentage of secondary structures. CLC main workbench analysis revealed a pattern length of 9 residues Sequence as DVSLVDGFN. Archschema analysis showed PF00314 as main Pfam domain of Thaumatin family, which was common in Ripening-associated protein Glucan endo-1, 3-beta-glucosidaseand some defense proteins. There were 53 domain of architecture related to TLP such as protein kinase, protein tyrosin kinase, probable lipid transfer, gag polypeptide of LTR copia-type too.

کلیدواژه ها:

Pathogenesis-Related proteins ، thaumatin-like protein (TLP) ، antifungal ، bioinformatics