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| Item Type: | Review |
|---|---|
| Title: | Cold-shock domains - abundance, structure, properties, and nucleic-acid binding |
| Creators Name: | Heinemann, U. and Roske, Y. |
| Abstract: | The cold-shock domain has a deceptively simple architecture but supports a complex biology. It is conserved from bacteria to man and has representatives in all kingdoms of life. Bacterial cold-shock proteins consist of a single cold-shock domain and some, but not all are induced by cold shock. Cold-shock domains in human proteins are often associated with natively unfolded protein segments and more rarely with other folded domains. Cold-shock proteins and domains share a five-stranded all-antiparallel β-barrel structure and a conserved surface that binds single-stranded nucleic acids, predominantly by stacking interactions between nucleobases and aromatic protein sidechains. This conserved binding mode explains the cold-shock domains' ability to associate with both DNA and RNA strands and their limited sequence selectivity. The promiscuous DNA and RNA binding provides a rationale for the ability of cold-shock domain-containing proteins to function in transcription regulation and DNA-damage repair as well as in regulating splicing, translation, mRNA stability and RNA sequestration. |
| Keywords: | Cold-Shock Domain, Cold-Shock Protein, RNA-Binding Domain, Nucleic-Acid Binding, Gene Regulation, OB Fold, Y-Box Binding Protein, Domain Fold, Protein Structure, Protein Stability and Folding |
| Source: | Cancers |
| ISSN: | 2072-6694 |
| Publisher: | MDPI |
| Volume: | 13 |
| Number: | 2 |
| Page Range: | 190 |
| Date: | 7 January 2021 |
| Official Publication: | https://doi.org/10.3390/cancers13020190 |
| PubMed: | View item in PubMed |
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