Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/13162
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Título : Binding of transcriptional activators to sigma 54 in the presence of the transition state analog ADP-aluminum fluoride: insights into activator mechanochemical action
Autor : 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
Palabras clave : Activators
Sigma 54
ADP · AlFx
AAA+ proteins
Fecha de publicación : 11-Jul-2001
Editor: Cold Spring Harbor Laboratory. Press
Citación : Genes and Development 15(17):2282-94
Resumen: 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.
Versión del editor: 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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