In Silico Analysis of Sucrose: Froctan 6- Froctose Transferase Gene in Triticum aestivum L.

Fallah Ziarani, Masoumeh; Safaeizadeh, Mehdi

doi:10.30473/cb.2022.64450.1881

In Silico Analysis of Sucrose: Froctan 6- Froctose Transferase Gene in Triticum aestivum L.

Document Type : Research Paper

Authors

¹ Ph.D. Student in Plant Biotechnology, Faculty of Life Science and Biotechnology, Shahid Beheshti University, Tehran, Iran.

² Assistant Prof., Faculty of Life Science and Biotechnology, Shahid Beheshti University, Tehran, Iran

10.30473/cb.2022.64450.1881

Abstract

Sucrose Froctan 6 fructosyl transferase is an enzyme that catalyzes the transfer of the fructosyl group from sucrose to various receptors. The importance of this protein is due to its role in increasing plant resistance against stresses. Due to the importance of sucrose transport in the cell, this gene was studied with the help of various databases and various bioinformatics software and it was compared with genes involved in the hydrolysis of O-glycosyl in wheat as well as genes of other plant species. Phylogenetic analysis divided 21 haplotypes into eight distinct groups. An exon was detected on the positive strand of this gene by FgenesH program and it was found that its predicted protein is 619 amino acids long. MapViewer revealed that the sequence carrying the Sucrose Froctan 6 fructosyl transferase (6-sft) access gene (JQ728011) is located on chromosome 4 of wheat. The isoelectric point (pI) of the target protein is 5.19, its net charge is -24 and examination of the Instability index showed that this protein has a long life. The molecular weight of Sucrose Froctan 6 fructosyl transferase (6-sft) protein was 6877.38 Da and ontologically, the 6-sft protein remains inside the cell. This protein has two protected domains PF00251 (Glyco-hydrolasy) and SSF75005 (Arabinana) at the N-terminus and a domain is SSF49899 (Cancanava) at the end of C. It was inferred that this protein was transported to the nucleus by the domain glyco-hydrolasy after synthesis in the cytoplasm and regulates O-glycosyle hydrolysis in wheat. Comparison of the secondary structure of the protein confirmed the existence of alpha plates. Three-dimensional modeling of this protein in wheat was performed by homology modeling method using Swiss Model database after selecting the appropriate model with high similarity that was extracted from PDB database. To validation of modeled structure and esterochemical analysis, Ramachandran plot was drawn and dihydral angles were calculated. Structural quality evaluation results showed that the proposed models are good quality and stability. The study of protein structure may help to understand protein function and the details of its structure can be useful in studies of the active site of the protein and docking.

Keywords

Main Subjects

Bioinformatics

References

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