Bordes, Patricia;
Wigneshweraraj, Siva R.;
Chaney, Matthew;
Dago, Angel E.;
Morett, Enrique;
Buck, Martin
Communication between Eσ54, promoter DNA and the conserved threonine residue in the GAFTGA motif of the PspF σ54‐dependent activator during transcription activation
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Medientyp:
E-Artikel
Titel:
Communication between Eσ54, promoter DNA and the conserved threonine residue in the GAFTGA motif of the PspF σ54‐dependent activator during transcription activation
Beteiligte:
Bordes, Patricia;
Wigneshweraraj, Siva R.;
Chaney, Matthew;
Dago, Angel E.;
Morett, Enrique;
Buck, Martin
Beschreibung:
<jats:title>Summary</jats:title><jats:p>Conversion of Eσ<jats:sup>54</jats:sup> closed promoter complexes to open promoter complexes requires specialized activators which are members of the AAA (ATPases Associated with various cellular Activities) protein family. The ATP binding and hydrolysis activity of Eσ<jats:sup>54</jats:sup> activators is used in an energy coupling reaction to remodel the Eσ<jats:sup>54</jats:sup> closed promoter complex and to overcome the σ<jats:sup>54</jats:sup>‐imposed block on open complex formation. The remodelling target for the AAA activator within the Eσ<jats:sup>54</jats:sup> closed complex includes a complex interface contributed to by Region I of σ<jats:sup>54</jats:sup>, core RNA polymerase and a promoter DNA fork junction structure, comprising the Eσ<jats:sup>54</jats:sup> regulatory centre. One σ<jats:sup>54</jats:sup> binding surface on Eσ<jats:sup>54</jats:sup> activators is a conserved sequence known as the GAFTGA motif. Here, we present a detailed characterization of the interaction between Region I of σ<jats:sup>54</jats:sup> and the <jats:italic>Escherichia coli</jats:italic> AAA σ<jats:sup>54</jats:sup> activator Phage shock protein F. Using Eσ<jats:sup>54</jats:sup> promoter complexes that mimic different conformations adopted by the DNA during open complex formation, we investigated the contribution of the conserved threonine residue in the GAFTGA motif to transcription activation. Our results suggest that the organization of the Eσ<jats:sup>54</jats:sup> regulatory centre, and in particular the conformation adopted by the σ<jats:sup>54</jats:sup> Region I and the DNA fork junction structure during open complex formation, is communicated to the AAA activator via the conserved T residue of the GAFTGA motif.</jats:p>