2024-03-28T18:50:58Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/131622021-12-28T15:44:08Zcom_10261_59com_10261_6col_10261_312
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
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