Abstract
The mode of packing for eukaryotic DNA is well established. A set of small basic proteins, the histones, is involved in the formation of compact DNA-protein particles in which the double-helical DNA is coiled around an octameric histone complex (Baldwin et al. 1975). A medium resolution structure of these “nucleosomes” has been obtained by crystallographic methods (Richmond et al. 1984). In bacteria, the mechanism for folding of the long circular DNA molecule into a compact form is much less clear. Although a number of proteins have been implicated for this function (Geider and Hoffmann-Berling 1981), a precise description of the composition of “bacterial chromatin” is not available.
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© 1986 Springer-Verlag Berlin Heidelberg
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Dijk, J., Reinhardt, R. (1986). The Structure of DNA-Binding Proteins from Eu- and Archaebacteria. In: Gualerzi, C.O., Pon, C.L. (eds) Bacterial Chromatin. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71266-1_15
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DOI: https://doi.org/10.1007/978-3-642-71266-1_15
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