Abstract
This chapter summarizes the structural details and functional properties of a representative selection of nucleoid-associated proteins (NAPs), consisting of FIS, H-NS, LRP, IHF, HU and Dps. Currently, high resolution structural information of the complete proteins is available for FIS, LRP, IHF, HU and Dps, while for H-NS structures have only been solved for the separate C- and N-terminal halves of the protein. In some cases, such as IHF or HU, structures of the proteins in complex with their target DNA have been determined. For the other proteins reasonable models describing the architecture of the respective protein-DNA complexes have been derived from biochemical and biophysical studies.
A common denominator for all the nucleoid-associated proteins is their property to induce structural deformations to the bound DNA. Each protein appears to affect DNA conformation or topology in a very specific way, however. Despite their general function in compacting DNA these differential properties are key to the high versatility of the NAPs as general and gene-specific regulators in the cell.
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Pul, Ü., Wagner, R. (2010). Nucleoid-Associated Proteins: Structural Properties. In: Dame, R.T., Dorman, C.J. (eds) Bacterial Chromatin. Springer, Dordrecht. https://doi.org/10.1007/978-90-481-3473-1_8
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