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Article

Binding of transcriptional activators to sigma 54 in the presence of the transition state analog ADP-aluminum fluoride: insights into activator mechanochemical action.

Genes & development - 1 Sept 2001

Chaney M, Grande R, Wigneshweraraj S R, Cannon W, Casaz P, Gallegos M T, Schumacher J, Jones S, Elderkin S, Dago A E, Morett E, Buck M

Abstract excerpt

Conformational changes in sigma 54 (sigma(54)) and sigma(54)-holoenzyme depend on nucleotide hydrolysis by an activator. We now show that sigma(54) and its holoenzyme bind to the central ATP-hydrolyzing domains of the transcriptional activators PspF and NifA in the presence of ADP-aluminum fluori...

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Identifiers

PMID: 11544185
DOI: 10.1101/gad.205501
PMCID: PMC312774

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-11544185-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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