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Review article2022Peer reviewedOpen access

Correlating multi-functional role of cold shock domain proteins with intrinsically disordered regions

Chaudhary, Amit; Chaurasia, Pankaj Kumar; Kushwaha, Sandeep; Chauhan, Pallavi; Chawade, Aakash; Mani, Ashutosh


Cold shock proteins (CSPs) are an ancient and conserved family of proteins. They are renowned for their role in response to low-temperature stress in bacteria and nucleic acid binding activities. In prokaryotes, cold and non -cold inducible CSPs are involved in various cellular and metabolic processes such as growth and development, osmotic oxidation, starvation, stress tolerance, and host cell invasion. In prokaryotes, cold shock condition re-duces cell transcription and translation efficiency. Eukaryotic cold shock domain (CSD) proteins are evolved form of prokaryotic CSPs where CSD is flanked by N-and C-terminal domains. Eukaryotic CSPs are multi-functional proteins. CSPs also act as nucleic acid chaperons by preventing the formation of secondary structures in mRNA at low temperatures. In human, CSD proteins play a crucial role in the progression of breast cancer, colon cancer, lung cancer, and Alzheimer's disease. A well-defined three-dimensional structure of intrinsically disordered re-gions of CSPs family members is still undetermined. In this article, intrinsic disorder regions of CSPs have been explored systematically to understand the pleiotropic role of the cold shock family of proteins.


Cold shock protein; CSPs; Cold shock domain; Stress protein; Intrinsically disordered regions

Published in

International Journal of Biological Macromolecules
2022, Volume: 220, pages: 743-753
Publisher: ELSEVIER

    Sustainable Development Goals

    SDG3 Ensure healthy lives and promote well-being for all at all ages

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    Biochemistry and Molecular Biology

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