Computational analysis of heat shock protein (HSP) in Citrus X Sinensis

Abstract

Heat shock proteins (HSPs) are molecular chaperones and one of the cell’s most important regulatory proteins present in all species. HSPs are a multigene family classified into six families according to their molecular weight range between 8KDa to 110KDa: HSP100, HSP90, HSP70, HSP60, small heat shock proteins (sHSPs), and ubiquitin. Citrus X Sinensis is very economical, and widely grown in the world. It is one of the best sources of nutrition, vitamin C, fiber, thiamine, folate, and antioxidants. It has a variety of health benefits i.e., protects against cell damage, boosts the immune system, heals wounds, etc. For highlighting the aspect of HSPs of citrus in computing protein, this work has great significance. Present studies are based on the identification and characterization of heat shock proteins in Citrus sinuses. In silico research was performed; Arabidopsis thaliana protein sequences of HSP60, HSP70 and HSP90 were used as a reference to identify these molecular chaperones in Citrus sinuses through Blast Phytozome. Furthermore, physiochemical properties, multiple sequence alignment, Multiple Expectation Maximization for Motif Elicitation (MEME) and phylogeny were constructed for 44 sequences of HSP60, 22 sequences of HSP70 and 23 for HSP90. The best expression of HSPs was found in Endoplasmic Reticulum. The findings of the present studies provide a good understanding of the HSP60, HSP70 and HSP90 families' function and expression site in the cell of Citrus sinuses. It also provides the basic knowledge for further investigations of the putative structure of dynamic proteins.