bEBPs (bacterial enhancer-binding proteins) are AAA+ (ATPase associated with various cellular activities) transcription activators that activate gene transcription through a specific bacterial σ factor, σ54. σ54–RNAP (RNA polymerase) binds to promoter DNA sites and forms a stable closed complex, unable to proceed to transcription. The closed complex must be remodelled using energy from ATP hydrolysis provided by bEBPs to melt DNA and initiate transcription. Recently, large amounts of structural and biochemical data have produced insights into how ATP hydrolysis within the active site of bEBPs is coupled to the re-modelling of the closed complex. In the present article, we review some of the key nucleotides, mutations and techniques used and how they have contributed towards our understanding of the function of bEBPs.
Dissecting the ATP hydrolysis pathway of bacterial enhancer-binding proteins
- Views Icon Views
- Share Icon Share
- Cite Icon Cite
Daniel Bose, Nicolas Joly, Tillmann Pape, Mathieu Rappas, Jorg Schumacher, Martin Buck, Xiaodong Zhang; Dissecting the ATP hydrolysis pathway of bacterial enhancer-binding proteins. Biochem Soc Trans 1 February 2008; 36 (1): 83–88. doi: https://doi.org/10.1042/BST0360083
Download citation file: