Please use this identifier to cite or link to this item:
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
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):
ISSN: 2282–2294
???metadata.dc.identifier.doi???: 10.1101/gad.205501
Citation: Genes and Development 15(17):2282-94
Appears in Collections:(EEZ) Artículos

Files in This Item:
There are no files associated with this item.
Show full item record

Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.