2024-03-28T11:17:31Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/131622021-12-28T15:44:08Zcom_10261_59com_10261_6col_10261_312
DIGITAL.CSIC
author
Chaney, Matthew
author
Grande, Ricardo
author
Wigneshweraraj, Siva R.
author
Cannon, Wendy
author
Casaz, Paul
author
Gallegos, María Trinidad
author
Schumacher, Jorg
author
Jones, Susan
author
Elderkin, Sarah
author
Dago, Angel Ernesto
author
Morett, Enrique
author
Buck, Martin
2009-05-22T10:35:19Z
2009-05-22T10:35:19Z
2001-07-11
Genes and Development 15(17):2282-94
2282–2294
http://hdl.handle.net/10261/13162
10.1101/gad.205501
11544185
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.
eng
closedAccess
Activators
Sigma 54
ADP · AlFx
AAA+ proteins
Binding of transcriptional activators to sigma 54 in the presence of the transition state analog ADP-aluminum fluoride: insights into activator mechanochemical action
artículo
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