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Dimerization and DNA-dependent aggregation of the Escherichia coli nucleoid protein and chaperone CbpA
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Cosgriff, Sarah, Chintakayala, Kiran, Chim, Ya Tsz A., Chen, Xinyong, Allen, Stephanie, Lovering, Andrew L. and Grainger, David C.. (2010) Dimerization and DNA-dependent aggregation of the Escherichia coli nucleoid protein and chaperone CbpA. Molecular Microbiology, Vol.77 (No.5). pp. 1289-1300. ISSN 0950-382X
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Official URL: http://dx.doi.org/10.1111/j.1365-2958.2010.07292.x
Abstract
The Escherichia coli curved DNA-binding protein A (CbpA) is a nucleoid-associated DNA-binding factor and chaperone that is expressed at high levels as cells enter stationary phase. Using a combination of genetics, biochemistry, structural modelling and single-molecule atomic force microscopy we have examined dimerization of, and DNA binding by, CbpA. Our data show that CbpA dimerization is driven by a hydrophobic surface comprising amino acid side chains W287 and L290 located on the same side of an alpha helix close to the C-terminus of CbpA. Derivatives of CbpA that are unable to dimerize are also unable to bind DNA. Free in solution, CbpA can exist as either a monomer or dimer. However, when bound to DNA, CbpA forms large aggregates that can protect DNA from degradation by nucleases. These CbpA-DNA aggregates are similar in morphology to protein-DNA complexes formed by the DNA-binding protein from starved cells (Dps), the only other stationary phase-specific nucleoid protein. Conversely, protein-DNA complexes formed by Fis, the major growth phase nucleoid protein, have a markedly different appearance.
| Item Type: | Journal Article |
|---|---|
| Subjects: | Q Science > QD Chemistry Q Science > QR Microbiology |
| Divisions: | Faculty of Science > Life Sciences (2010- ) > Biological Sciences ( -2010) |
| Journal or Publication Title: | Molecular Microbiology |
| Publisher: | Wiley-Blackwell Publishing Ltd. |
| ISSN: | 0950-382X |
| Date: | September 2010 |
| Volume: | Vol.77 |
| Number: | No.5 |
| Number of Pages: | 12 |
| Page Range: | pp. 1289-1300 |
| Identification Number: | 10.1111/j.1365-2958.2010.07292.x |
| Status: | Peer Reviewed |
| Publication Status: | Published |
| Access rights to Published version: | Restricted or Subscription Access |
| Funder: | Wellcome Trust, Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC) |
| Grant number: | BB/H010289/1 (BBSRC) |
| URI: | http://wrap.warwick.ac.uk/id/eprint/5296 |
Data sourced from Thomson Reuters' Web of Knowledge
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