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Vol. 15, No. 17, pp. 2282-2294, September 1, 2001
1 Department of Biology and Biochemistry, Faculty of Life
Sciences, Sir Alexander Fleming Building, Imperial College of Science
Technology and Medicine, London SW7 2AZ, UK; 2 Departamento de
Reconocimiento Molecular y Bioestructura, Instituto de Biotecnología,
Universidad Nacional Autónoma de México, AP 510-3, Cuernavaca,
Morelos 62250, México
Conformational changes in sigma 54 (
54) and
54-holoenzyme depend on nucleotide hydrolysis by an
activator. We now show that 54 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
54 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
54 Region I. ADP-aluminum fluoride-dependent interactions
and consideration of other AAA+ proteins provide insight into activator
mechanochemical action.
[Key Words: Sigma 54; activators; transcription; ADP · AlFx; AAA+ proteins]
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