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

Chaudhary, Amit (author)
Indian Institute of Technology Bombay
Chaurasia, Pankaj Kumar (author)
Kushwaha, Sandeep (author)
University of Hyderabad
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Chauhan, Pallavi (author)
Lund University,Lunds universitet,Evolutionär ekologi,Biologiska institutionen,Naturvetenskapliga fakulteten,MEMEG,Molekylär cellbiologi,Evolutionary ecology,Department of Biology,Faculty of Science,Molecular Cell Biology
Chawade, Aakash (author)
Sveriges lantbruksuniversitet,Swedish University of Agricultural Sciences,Institutionen för växtförädling,Department of Plant Breeding
Mani, Ashutosh (author)
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 (creator_code:org_t)
 
Elsevier BV, 2022
2022
English 11 s.
In: International Journal of Biological Macromolecules. - : Elsevier BV. - 0141-8130 .- 1879-0003. ; 220, s. 743-753
  • Research review (peer-reviewed)
Abstract Subject headings
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  • 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.

Subject headings

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)

Keyword

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

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