Abstract
DNA binding proteins have attracted the attention of molecular biologists during the past few years, after it became clear that, both in prokaryotes and in eukaryotes, control of gene expression is often mediated by the interaction of regulatory proteins with defined DNA sequences.1,2 A comparison of the DNA binding sites of several prokaryotic regulatory proteins reveals a helix-turn-helix motif that exhibits a high degree of conservation in the primary structure and is supposed to interact with the B-form of the DNA double helix.1 The DNA sequences that are recognised by these regulatory proteins also show a striking similarity, independently of whether they mediate positive or negative modulation of transcription — in other words, activation or repression of genes.3 In addition, these DNA sequences exhibit limited inverted symmetry, reflecting the dimeric nature of the regulatory proteins.4 From these and similar data the idea of a ‘recognition code’ or a ‘regulatory code’ is arising, which implies the existence of a set of limited rules governing the interaction of the amino acid side-chains in regulatory proteins with the edges of the base pairs in the DNA double helix.1,5
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Further Reading
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© 1987 John M. Walker and Wim Gaastra
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Beato, M. (1987). DNA Footprinting and Related Techniques for Analysing Protein-DNA Interactions. In: Walker, J.M., Gaastra, W. (eds) Techniques in Molecular Biology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9799-5_15
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DOI: https://doi.org/10.1007/978-1-4615-9799-5_15
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