ArticleNucleic acids research2017
RNA binding and chaperone activity of the E. coli cold-shock protein CspA.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 57 citations in OpenAlex.
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- The Cold Shock Protein CspB fromInternational journal of molecular sciences · 2026Article
- Methionine Oxidation Footprinting in Intact Proteins (MOFIP) Using Top-Down Proteomics.Proteomics · 2025Article
- A Proteomic View on Persistence of Yersinia pestis in Tap Water Microcosm.Current microbiology · 2025Article
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- Horizontally acquired CSP genes contribute to wheat adaptation and improvement.Nature plants · 2025Article
- PRESERVE: adding variable flip-angle excitation to transverse relaxation-optimized NMR spectroscopy.Magnetic resonance (Gottingen, Germany) · 2024Article
- A high-throughput search for intracellular factors that affect RNA folding identifiesRNA biology · 2024Article
- Microproteins-Discovery, structure, and function.Proteomics · 2023Review
- Analysis of Osmotic Tolerance, Physiological Characteristics, and Gene Expression ofACS omega · 2023Article
- A general overview of the multifactorial adaptation to cold: biochemical mechanisms and strategies.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023Review
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- c-di-GMP regulates activity of the PlzA RNA chaperone from the Lyme disease spirochete.Molecular microbiology · 2023Article
- Pan-metagenome reveals the abiotic stress resistome of cigar tobacco phyllosphere microbiome.Frontiers in plant science · 2023Article
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- Acetylation of CspC Controls the Las Quorum-Sensing System through Translational Regulation ofmBio · 2022Article
- Unraveling the Role of Acetic Acid Bacteria Comparing Two Acetification Profiles From Natural Raw Materials: A Quantitative Approach inFrontiers in microbiology · 2022Article
- Genome mining reveals abiotic stress resistance genes in plant genomes acquired from microbesFrontiers in plant science · 2022Article
Corrections and comments
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Authors and funding
13 authors at 7 institutions in 2 countries.
Funding
Abstract
Ensuring the correct folding of RNA molecules in the cell is of major importance for a large variety of biological functions. Therefore, chaperone proteins that assist RNA in adopting their functionally active states are abundant in all living organisms. An important feature of RNA chaperone proteins is that they do not require an external energy source to perform their activity, and that they interact transiently and non-specifically with their RNA targets. So far, little is known about the mechanistic details of the RNA chaperone activity of these proteins. Prominent examples of RNA chaperones are bacterial cold shock proteins (Csp) that have been reported to bind single-stranded RNA and DNA. Here, we have used advanced NMR spectroscopy techniques to investigate at atomic resolution the RNA-melting activity of CspA, the major cold shock protein of Escherichia coli, upon binding to different RNA hairpins. Real-time NMR provides detailed information on the folding kinetics and folding pathways. Finally, comparison of wild-type CspA with single-point mutants and small peptides yields insights into the complementary roles of aromatic and positively charged amino-acid side chains for the RNA chaperone activity of the protein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.