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

Chaudhary, Amit ; Chaurasia, Pankaj Kumar ; Kushwaha, Sandeep LU ; Chauhan, Pallavi LU ; Chawade, Aakash LU and Mani, Ashutosh (2022) In International Journal of Biological Macromolecules 220. p.743-753
Abstract

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... (More)

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.

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organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Cold shock domain, Cold shock protein, CSPs, Intrinsically disordered regions, Stress protein
in
International Journal of Biological Macromolecules
volume
220
pages
11 pages
publisher
Elsevier
external identifiers
  • scopus:85136245380
  • pmid:35987358
ISSN
0141-8130
DOI
10.1016/j.ijbiomac.2022.08.100
language
English
LU publication?
yes
id
273d118a-ed4f-42c6-b24e-95d9ce835d37
date added to LUP
2022-10-06 14:56:15
date last changed
2024-06-13 19:58:46
@article{273d118a-ed4f-42c6-b24e-95d9ce835d37,
  abstract     = {{<p>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.</p>}},
  author       = {{Chaudhary, Amit and Chaurasia, Pankaj Kumar and Kushwaha, Sandeep and Chauhan, Pallavi and Chawade, Aakash and Mani, Ashutosh}},
  issn         = {{0141-8130}},
  keywords     = {{Cold shock domain; Cold shock protein; CSPs; Intrinsically disordered regions; Stress protein}},
  language     = {{eng}},
  pages        = {{743--753}},
  publisher    = {{Elsevier}},
  series       = {{International Journal of Biological Macromolecules}},
  title        = {{Correlating multi-functional role of cold shock domain proteins with intrinsically disordered regions}},
  url          = {{http://dx.doi.org/10.1016/j.ijbiomac.2022.08.100}},
  doi          = {{10.1016/j.ijbiomac.2022.08.100}},
  volume       = {{220}},
  year         = {{2022}},
}