Journal
EMBO JOURNAL
Volume 25, Issue 16, Pages 3784-3790Publisher
WILEY
DOI: 10.1038/sj.emboj.7601261
Keywords
activator-polymerase complex; DNA wrapping; FIS; RNA polymerase; torsional transmission
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Funding
- Medical Research Council [MC_U105184288] Funding Source: Medline
- MRC [MC_U105184288] Funding Source: UKRI
- Medical Research Council [MC_U105184288] Funding Source: researchfish
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Using high-resolution atomic force microscopy (AFM) we show that in a ternary complex of an activator protein, FIS, and RNA polymerase containing the sigma(70) specificity factor at the Escherichia coli tyrT promoter the polymerase and the activator form discrete, but connected, subcomplexes in close proximity. This is the first time that a ternary complex between an activator, a sigma(70) polymerase holoenzyme and promoter DNA has been visualised. Individually FIS and RNA polymerase wrap similar to 80 and 150 bp of promoter DNA, respectively. We suggest that the architecture of the ternary complex provides a general paradigm for the facilitation of direct, but weak, interactions between polymerase and an activator.
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