ArticleNucleic acids research2006
Recognition of T-rich single-stranded DNA by the cold shock protein Bs-CspB in solution.
Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 48 citations in OpenAlex.
- Quantifying Ligand-to-Protein Distances in Complex Environments Using IntermolecularChembiochem : a European journal of chemical biology · 2026Article
- 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
- Himalayan Microbiomes for Agro-environmental Sustainability: Current Perspectives and Future Challenges.Microbial ecology · 2022Review
- Fluorine NMR Spectroscopy Enables to Quantify the Affinity Between DNA and Proteins in Cell Lysate.Chembiochem : a European journal of chemical biology · 2021Article
- Impact of crowded environments on binding between protein and single-stranded DNA.Scientific reports · 2021Article
- Review
- Insights into Protein Stability in Cell Lysate byChembiochem : a European journal of chemical biology · 2020Article
- One evolutionarily selected amino acid variation is sufficient to provide functional specificity in the cold shock protein paralogs of Staphylococcus aureus.Molecular microbiology · 2020Article
- The regulon of the RNA chaperone CspA and its auto-regulation in Staphylococcus aureus.Nucleic acids research · 2018Article
- Electronic Structures of LNA Phosphorothioate Oligonucleotides.Molecular therapy. Nucleic acids · 2017Article
- Unusual dimerization of a BcCsp mutant leads to reduced conformational dynamics.The FEBS journal · 2017Article
- RNA binding and chaperone activity of the E. coli cold-shock protein CspA.Nucleic acids research · 2017Article
- Quantum mechanical studies of DNA and LNA.Nucleic acid therapeutics · 2014Article
- Mechanisms of Lin28-mediated miRNA and mRNA regulation--a structural and functional perspective.International journal of molecular sciences · 2013Review
- Single-stranded DNA-binding proteins: multiple domains for multiple functions.Structure (London, England : 1993) · 2013Review
- The Lin28 cold-shock domain remodels pre-let-7 microRNA.Nucleic acids research · 2012Article
- RNA single strands bind to a conserved surface of the major cold shock protein in crystals and solution.RNA (New York, N.Y.) · 2012Article
- Influence of the stability of a fused protein and its distance to the amyloidogenic segment on fibril formation.PloS one · 2010Article
- Crystallization and X-ray structure of cold-shock protein E from Salmonella typhimurium.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- Relative stabilities of conserved and non-conserved structures in the OB-fold superfamily.International journal of molecular sciences · 2009Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cold shock proteins (CSP) belong to the family of single-stranded nucleic acid binding proteins with OB-fold. CSP are believed to function as 'RNA chaperones' and during anti-termination. We determined the solution structure of Bs-CspB bound to the single-stranded DNA (ssDNA) fragment heptathymidine (dT7) by NMR spectroscopy. Bs-CspB reveals an almost invariant conformation when bound to dT7 with only minor reorientations in loop beta1-beta2 and beta3-beta4 and of few aromatic side chains involved in base stacking. Binding studies of protein variants and mutated ssDNA demonstrated that Bs-CspB associates with ssDNA at almost diffusion controlled rates and low sequence specificity consistent with its biological function. A variation of the ssDNA affinity is accomplished solely by changes of the dissociation rate. 15N NMR relaxation and H/D exchange experiments revealed that binding of dT7 increases the stability of Bs-CspB and reduces the sub-nanosecond dynamics of the entire protein and especially of loop beta3-beta4.
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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.