Cold-Shock Domains—Abundance, Structure, Properties, and Nucleic-Acid Binding
Crystallography, Max Delbrück Center for Molecular Medicine, 13125 Berlin, Germany
Author to whom correspondence should be addressed.
Received: 22 December 2020
Revised: 5 January 2021
Accepted: 6 January 2021
Published: 7 January 2021
Proteins are composed of compact domains, often of known three-dimensional structure, and natively unstructured polypeptide regions. The abundant cold-shock domain is among the set of canonical nucleic acid-binding domains and conserved from bacteria to man. Proteins containing cold-shock domains serve a large variety of biological functions, which are mostly linked to DNA or RNA binding. These functions include the regulation of transcription, RNA splicing, translation, stability and sequestration. Cold-shock domains have a simple architecture with a conserved surface ideally suited to bind single-stranded nucleic acids. Because the binding is mostly by non-specific molecular interactions which do not involve the sugar-phosphate backbone, cold-shock domains are not strictly sequence-specific and do not discriminate reliably between DNA and RNA. Many, but not all functions of cold shock-domain proteins in health and disease can be understood based of the physical and structural properties of their cold-shock domains.