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. 1991 Sep;10(9):2589–2594. doi: 10.1002/j.1460-2075.1991.tb07800.x

Flexibility of the DNA enhances promoter affinity of Escherichia coli RNA polymerase.

W Werel 1, P Schickor 1, H Heumann 1
PMCID: PMC452957  PMID: 1868834

Abstract

Two types of mechanisms are discussed for the formation of active protein-DNA complexes: contacts with specific bases and interaction via specific DNA structures within the cognate DNA. We have studied the effect of a single nucleoside deletion on the interaction of Escherichia coli RNA polymerase with a strong promoter. This study reveals three patterns of interaction which can be attributed to different sites of the promoter, (i) direct base contact with the template strand in the '-35 region' (the 'recognition domain'), (ii) a DNA structure dependent interaction in the '-10 region' (the 'melting domain'), and (iii) an interaction which is based on a defined spatial relationship between the two domains of a promoter, namely the 'recognition domain' and the 'melting domain'.

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Selected References

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