Chaperones, vital molecules in microbes
Subject Areas : Molecular genetics of microorganisms
Kimia
Golestanfar
1
(Ph.D Student,Department of Microbiology, Faculty of Basic Siences, Shahrekord Branch, Islamic Azad University, Shahrekord, Iran)
Keywords: Chaperone, folding, temperature stress,
Abstract :
Molecular chaperones are highly conserved proteins that promote proper folding of other proteins inside the body. Diverse chaperone systems contribute to protein folding and translocation, assembly of oligomeric complexes, and recovery from stress-induced unfolding. A fundamental function of molecular chaperones is to inhibit nonproductive protein interactions by recognizing and protecting hydrophobic surfaces that are exposed during folding or following proteotoxic stress. Therefore, chaperones are of special importance in cellular systems, which are discussed in this review article about these molecules and their mechanisms of action. Also, changes in gene expression in oxidative conditions in bacteria will be discussed in order to tolerate environmental conditions.
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