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| Item Type: | Article |
|---|---|
| Title: | Recognition of T-rich single-stranded DNA by the cold shock protein Bs-CspB in solution |
| Creators Name: | Zeeb, M., Max, K.E.A., Weininger, U., Loew, C., Sticht, H. and Balbach, J. |
| 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 {beta}1-{beta}2 and {beta}3-{beta}4 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 {beta}3-{beta}4. |
| Keywords: | Bacillus Subtilis, Bacterial Proteins, Biomolecular Nuclear Magnetic Resonance, DNA Mutational Analysis, Deuterium Exchange Measurement, Kinetics, Molecular Models, Protein Conformation, Single-Stranded DNA, Thermodynamics, Thymidine |
| Source: | Nucleic Acids Research |
| ISSN: | 0305-1048 |
| Publisher: | Oxford University Press |
| Volume: | 34 |
| Number: | 16 |
| Page Range: | 4561-4571 |
| Date: | 2006 |
| Official Publication: | https://doi.org/10.1093/nar/gkl376 |
| PubMed: | View item in PubMed |
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