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Review

Cold shock proteins: Orchestrating cellular defense in response to low temperatures
Mrinmoy Ghosh12
,
Myeongyeon Shin2
,
Young-Ok Son23*
1Department of Biotechnology, School of Bio, Chemical and Processing Engineering (SBCE), Kalasalingam Academy of Research and Educational, Krishnankoil 626126, India
2Department of Animal Biotechnology, Faculty of Biotechnology, College of Applied Life Sciences, Jeju National University, Jeju Special Self-Governing Province 63243, Republic of Korea
3Interdisciplinary Graduate Program in Advanced Convergence Technology and Science, Jeju National University, Jeju Special Self-Governing Province 63243, Republic of Korea
*Corresponding Author
30 April 2024. pp. 12-19
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Abstract

Living organisms face formidable challenges in frigid environments, such as the cryosphere, where temperature variations significantly impact their survival. Psychrophiles, resilient microorganisms inhabiting frozen realms, have evolved adaptive strategies to thrive in these harsh conditions. Furthermore, both other prokaryotic and eukaryotic cells also display an adaptive cold shock response when exposed to a sudden decrease in temperature. The cellular response to sudden temperature decreases involves the induction of cold shock proteins (CSPs). CSPs, recognized for their pivotal role in cellular adaptation to cold stress, exhibit structural characteristics that make them intriguing subjects for study. This analysis delves into the conformational stability, folding kinetics, and functional aspects of CSPss, emphasizing their unique cold shock domain (CSD). CSPs lack disulfide bonds and cis-peptides, simplifying the study of their folding mechanisms. The CspA, a major contributor to protein synthesis during cold stress. The CSP family's genetic manipulations underscore their critical role in bacterial adaptation to cold environments. The CSD, a hallmark of CSPs, forms an antiparallel five-stranded β-barrel, retaining nucleic acid-binding capabilities crucial for cold adaptation. The RNA-binding site within the CSD plays a pivotal role in stable RNA-protein complex formation. CSPs’ flexibility contributes to functional versatility, enabling them to act as RNA chaperones, aiding in proper RNA folding. Oligomeric structures formed by CSPs, varying in states such as dimers or trimers, are associated with their functional activities, particularly in RNA chaperone functions. This comprehensive analysis provides insights into the biophysical properties of CSPs, shedding light on their structural features, RNA interactions, and functional adaptability. Understanding the adaptive mechanisms of microorganisms in extremely cold environments and towards the cold shock response, particularly the role of CSPs, contributes to our knowledge of cellular homeostasis in such conditions.

Keywords
Cold shock proteins
Cold shock domain
β-strands
RNA-binding site
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Information
  • Publisher :Jeju Journal of Island Sciences
  • Publisher(Ko) :제주섬과학회지
  • Journal Title :Jeju Journal of Island Sciences
  • Journal Title(Ko) :제주섬과학회지
  • Volume : 1
  • No :1
  • Pages :12-19
  • Received Date : 2024-02-15
  • Revised Date : 2024-03-11
  • Accepted Date : 2024-03-13
  • DOI :https://doi.org/10.23264/JJIS.2024.1.1.012
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