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Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/13162
Title: Binding of transcriptional activators to sigma 54 in the presence of the transition state analog ADP-aluminum fluoride: insights into activator mechanochemical action
Authors: Chaney, Matthew; Grande, Ricardo; Wigneshweraraj, Siva R.; Cannon, Wendy; Casaz, Paul; Gallegos, María Trinidad; Schumacher, Jorg; Jones, Susan; Elderkin, Sarah; Dago, Angel Ernesto; Morett, Enrique; Buck, Martin
Keywords: Activators
Sigma 54
ADP · AlFx
AAA+ proteins
Issue Date: 11-Jul-2001
Publisher: Cold Spring Harbor Laboratory. Press
Citation: Genes and Development 15(17):2282-94
Abstract: Conformational changes in sigma 54(σ54) and σ54-holoenzyme depend on nucleotide hydrolysis by an activator. We now show that σ54 and its holoenzyme bind to the central ATP-hydrolyzing domains of the transcriptional activators PspF and NifA in the presence of ADP–aluminum fluoride, an analog of ATP in the transition state for hydrolysis. Direct binding of σ54 Region I to activator in the presence of ADP–aluminum fluoride was shown and inferred from in vivo suppression genetics. Energy transduction appears to occur through activator contacts to σ54 Region I. ADP–aluminum fluoride-dependent interactions and consideration of other AAA+ proteins provide insight into activator mechanochemical action.
Publisher version (URL): http://dx.doi.org/10.1101/gad.205501
URI: http://hdl.handle.net/10261/13162
ISSN: 2282–2294
DOI: 10.1101/gad.205501
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