ArticleProtein science : a publication of the Protein Society2003
Single-stranded DNA binding of the cold-shock protein CspB from Bacillus subtilis: NMR mapping and mutational characterization.
Article in Protein science : a publication of the Protein Society, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 50 citations in OpenAlex.
- Targeting an essentialiScience · 2023Article
- 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
- Pleiotropic roles of cold shock proteins with special emphasis on unexplored cold shock protein member of Plasmodium falciparum.Malaria journal · 2020Review
- CspA regulation of Staphylococcus aureus carotenoid levels and σMolecular microbiology · 2019Article
- Identification of LIN28B-bound mRNAs reveals features of target recognition and regulation.RNA biology · 2013Article
- Early turn formation and chain collapse drive fast folding of the major cold shock protein CspA of Escherichia coli.Biochemistry · 2012Article
- The Lin28 cold-shock domain remodels pre-let-7 microRNA.Nucleic acids research · 2012Article
- Inhibition of gluconeogenic genes by calcium-regulated heat-stable protein 1 via repression of peroxisome proliferator-activated receptor α.The Journal of biological chemistry · 2011Article
- Structural models of protein-DNA complexes based on interface prediction and docking.Current protein & peptide science · 2011Article
- Structure-functional analyses of CRHSP-24 plasticity and dynamics in oxidative stress response.The Journal of biological chemistry · 2011Article
- Autocatalytic genetic networks modeled by piecewise-deterministic Markov processes.Journal of mathematical biology · 2010Article
- Crystallization and X-ray structure of cold-shock protein E from Salmonella typhimurium.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- Characterization of protein secondary structure from NMR chemical shifts.Progress in nuclear magnetic resonance spectroscopy · 2009Article
- A folded and functional protein domain in an amyloid-like fibril.Protein science : a publication of the Protein Society · 2008Article
- Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008Article
- Sequence specificity of single-stranded DNA-binding proteins: a novel DNA microarray approach.Nucleic acids research · 2007Article
- Recognition of T-rich single-stranded DNA by the cold shock protein Bs-CspB in solution.Nucleic acids research · 2006Article
- CspA regulates pigment production in Staphylococcus aureus through a SigB-dependent mechanism.Journal of bacteriology · 2005Article
- Bacterial cold shock responses.Science progress · 2003Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cold-shock proteins (CSPs) bind to single-stranded nucleic acids, thereby acting as a "RNA chaperone." To gain deeper insights into the rather unspecific nature of ssDNA/RNA binding, we characterized the binding interface of CspB from Bacillus subtilis to a 25-mer of ssDNA (Y-Box25) using heteronuclear 2D NMR spectroscopy. Seventeen residues, including eight out of nine aromatic amino acids, are directly involved in the Y-Box25 interaction and were identified by extreme line broadening of their cross-peaks. Eight residues belong to the earlier proposed RNP binding motifs. A second set of seven backbone amides becomes evident by major chemical shift perturbations reporting remote conformational rearrangements upon binding. These residues are located in loop beta3-beta4 and loopbeta4-beta5, and include Ile18. The individual contributions of the so-identified residues were examined by fluorescence titration experiments of 15 CspB variants. Phenylalanine substitutions in- and outside the RNP motifs significantly reduce the binding affinity. Unrestricted possible backbone conformations of loop beta3-beta4 also markedly contribute to binding. Stopped-flow fluorescence kinetics revealed that the different binding affinities of CspB variants are determined by the dissociation rate, whereas the association rate remains unchanged. This might be of importance for the "RNA chaperone" activity of CspB.
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