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FEBS Open Bio. 2012 Apr 14;2:89-92. doi: 10.1016/j.fob.2012.04.002. Print 2012.

Formation of MgF3 (-)-dependent complexes between an AAA(+) ATPase and σ(54.).

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Division of Cell and Molecular Biology, Sir Alexander Fleming Building, Imperial College London, Exhibition Road, London SW7 2AZ, UK.


The widely distributed bacterial σ(54)-dependent transcription regulates pathogenicity and numerous adaptive responses in diverse bacteria. Formation of the σ(54)-dependent open promoter complex is a multi-step process driven by AAA(+) ATPases. Non-hydrolysable nucleotide analogues are particularly suitable for studying such complexity by capturing various intermediate states along the energy coupling pathway. Here we report a novel ATP analogue, ADP-MgF3 (-), which traps an AAA(+) ATPase with its target σ(54). The MgF3 (-)-dependent complex is highly homogeneous and functional assays suggest it may represent an early transcription intermediate state valuable for structural studies.


AAA+ ATPase; Nucleotide analogue; PspF; Transcription; bEBP; σ54

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