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RNA polymerase and an activator form discrete subcomplexes in a transcription initiation complex
Author(s) -
Maurer Sebastian,
Fritz Jürgen,
Muskhelishvili Georgi,
Travers Andrew
Publication year - 2006
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7601261
Subject(s) - biology , rna polymerase ii , transcription factor ii d , transcription (linguistics) , polymerase , genetics , rna polymerase , rna polymerase ii holoenzyme , transcription factor ii f , microbiology and biotechnology , rna , promoter , gene , gene expression , linguistics , philosophy
Using high‐resolution atomic force microscopy (AFM) we show that in a ternary complex of an activator protein, FIS, and RNA polymerase containing the σ 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 σ 70 polymerase holoenzyme and promoter DNA has been visualised. Individually FIS and RNA polymerase wrap ∼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.