Activation of RelA by pppGpp as the basis for its differential toxicity over ppGpp in Escherichia coli

Loading...
Thumbnail Image
Date
2020-01
Journal Title
Journal ISSN
Volume Title
Publisher
Indian Academy of Sciences
Abstract
Intrinsically disordered proteins (IDPs) are highly flexible and undergo disorder to order transition uponbinding. They are highly abundant in human proteomes and play critical roles in cell signaling and regulatoryprocesses. This review mainly focuses on the dynamics of disordered proteins including their conformationalheterogeneity, protein–protein interactions, and the phase transition of biomolecular condensates that arecentral to various biological functions. Besides, the role of RNA-mediated chaperones in protein folding andstability of IDPs were also discussed. Finally, we explored the dynamic binding interface of IDPs as noveltherapeutic targets and the effect of small molecules on their interactions.
Description
Keywords
(p)ppGpp, GppA, SpoT, RelA, stringent response
Citation
Sanyal Rajeshree, Harinarayanan Rajendran. Activation of RelA by pppGpp as the basis for its differential toxicity over ppGpp in Escherichia coli. Journal of Biosciences. 2020 Jan; : 1-13