Helmholtz Gemeinschaft


Cold-shock domains - abundance, structure, properties, and nucleic-acid binding

PDF (Article) - Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader

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
Page Range:190
Date:7 January 2021
Official Publication:https://doi.org/10.3390/cancers13020190
PubMed:View item in PubMed

Repository Staff Only: item control page


Downloads per month over past year

Open Access
MDC Library