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[논문] Cold shock proteins: Orchestrating cellular defense in response to low temperatures

Jeju Journal of Island Sciences

EISSN: 3022-9456

1(1)

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

Mrinmoy Ghosh, Myeongyeon Shin and Young-Ok Son*

https://doi.org/10.23264/JJIS.2024.1.1.012