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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 CSIC ORCID ; 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 | DOI: | 10.1101/gad.205501 | ISSN: | 2282–2294 |
Aparece en las colecciones: | (EEZ) Artículos |
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