Cold-Shock Domains—Abundance, Structure, Properties, and Nucleic-Acid Binding
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-...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-01-01
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| Series: | Cancers |
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| Online Access: | https://www.mdpi.com/2072-6694/13/2/190 |
| _version_ | 1797415330492973056 |
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| author | Udo Heinemann Yvette Roske |
| author_facet | Udo Heinemann Yvette Roske |
| author_sort | Udo Heinemann |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-09T05:46:10Z |
| format | Article |
| id | doaj.art-71399636773a45f3875d50c348be504e |
| institution | Directory Open Access Journal |
| issn | 2072-6694 |
| language | English |
| last_indexed | 2024-03-09T05:46:10Z |
| publishDate | 2021-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Cancers |
| spelling | doaj.art-71399636773a45f3875d50c348be504e2023-12-03T12:20:51ZengMDPI AGCancers2072-66942021-01-0113219010.3390/cancers13020190Cold-Shock Domains—Abundance, Structure, Properties, and Nucleic-Acid BindingUdo Heinemann0Yvette Roske1Crystallography, Max Delbrück Center for Molecular Medicine, 13125 Berlin, GermanyCrystallography, Max Delbrück Center for Molecular Medicine, 13125 Berlin, GermanyThe 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.https://www.mdpi.com/2072-6694/13/2/190cold-shock domaincold-shock proteinRNA-binding domainnucleic-acid bindinggene regulationOB fold |
| spellingShingle | Udo Heinemann Yvette Roske Cold-Shock Domains—Abundance, Structure, Properties, and Nucleic-Acid Binding Cancers cold-shock domain cold-shock protein RNA-binding domain nucleic-acid binding gene regulation OB fold |
| title | Cold-Shock Domains—Abundance, Structure, Properties, and Nucleic-Acid Binding |
| title_full | Cold-Shock Domains—Abundance, Structure, Properties, and Nucleic-Acid Binding |
| title_fullStr | Cold-Shock Domains—Abundance, Structure, Properties, and Nucleic-Acid Binding |
| title_full_unstemmed | Cold-Shock Domains—Abundance, Structure, Properties, and Nucleic-Acid Binding |
| title_short | Cold-Shock Domains—Abundance, Structure, Properties, and Nucleic-Acid Binding |
| title_sort | cold shock domains abundance structure properties and nucleic acid binding |
| topic | cold-shock domain cold-shock protein RNA-binding domain nucleic-acid binding gene regulation OB fold |
| url | https://www.mdpi.com/2072-6694/13/2/190 |
| work_keys_str_mv | AT udoheinemann coldshockdomainsabundancestructurepropertiesandnucleicacidbinding AT yvetteroske coldshockdomainsabundancestructurepropertiesandnucleicacidbinding |