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

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 processe...

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Bibliographic Details
Published inInternational journal of biological macromolecules Vol. 220; pp. 743 - 753
Main Authors Chaudhary, Amit, Chaurasia, Pankaj Kumar, Kushwaha, Sandeep, Chauhan, Pallavi, Chawade, Aakash, Mani, Ashutosh
Format Journal Article
LanguageEnglish
Published Elsevier B.V 01.11.2022
Subjects
Biochemistry and Molecular Biology
Biokemi och molekylärbiologi
Biologi
Biological Sciences
Cold shock domain
Cold shock protein
CSPs
Intrinsically disordered regions
Natural Sciences
Naturvetenskap
Stress protein
Stress protein
Intrinsically disordered regions
YB1
CSPs
Cold shock protein
CARHSP1
FASTpp
NMR
CSD
PIP
G3BP1
Cold shock domain
IDPs
CHSP1
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Summary: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 reduces 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 regions 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.
Bibliography:ObjectType-Article-2
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ISSN:0141-8130
1879-0003
1879-0003
DOI:10.1016/j.ijbiomac.2022.08.100