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Abstract

ABSTRACT:The Universal stress protein appears to belong to all stress and starvation stimulons under the inclusive regulation of gene expression. It has been suggested that Usp proteins have different physiological functions that reprogram the cell towards defense and escape during cellular stress. In this study Protein interaction network (PIN) analysis was used to predict its mechanism of molecular action. The PIN of Universal stress protein was constructed by Cytoscape and the function modules identified by gene ontology (GO) enrichment analysis based on molecular complex detection (MCODE). The PIN of Universal stress protein has scale-free, small world and modular properties.Based on analysis of these function modules, the mechanism of Universal stress protein is proposed.The protein-protein interactions information of Universal stress protein is connected to the protein secretion pathway, apoptosis, cell division, cell shape and gene regulation. These results will serve as a distinctive resource to present a physical map of protein profile of bacteria under stress condition, drug targeting and the development of novel therapeutics.