PMID:12601152
| Citation |
Bordes, P, Wigneshweraraj, SR, Schumacher, J, Zhang, X, Chaney, M and Buck, M (2003) The ATP hydrolyzing transcription activator phage shock protein F of Escherichia coli: identifying a surface that binds sigma 54. Proc. Natl. Acad. Sci. U.S.A. 100:2278-83 |
|---|---|
| Abstract |
Members of the protein family called ATPases associated with various cellular activities (AAA(+)) play a crucial role in transforming chemical energy into biological events. AAA(+) proteins are complex molecular machines and typically form ring-shaped oligomeric complexes that are crucial for ATPase activity and mechanism of action. The Escherichia coli transcription activator phage shock protein F (PspF) is an AAA(+) mechanochemical enzyme that functions to sense and relay the energy derived from nucleoside triphosphate hydrolysis to catalyze transcription by the sigma(54)-RNA polymerase. Closed promoter complexes formed by the sigma(54)-RNA polymerase are substrates for the action of PspF. By using a protein fragmentation approach, we identify here at least one sigma(54)-binding surface in the PspF AAA(+) domain. Results suggest that ATP hydrolysis by PspF is coupled to the exposure of at least one sigma(54)-binding surface. This nucleotide hydrolysis-dependent presentation of a substrate binding surface can explain why complexes that form between sigma(54) and PspF are transient and could be part of a mechanism used generally by other AAA(+) proteins to regulate activity. |
| Links |
PubMed PMC151331 Online version:10.1073/pnas.0537525100 |
| Keywords |
Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; Amino Acid Motifs; Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Base Sequence; DNA/metabolism; DNA-Binding Proteins; DNA-Directed RNA Polymerases/metabolism; Deoxyribonuclease I/chemistry; Deoxyribonuclease I/metabolism; Escherichia coli/metabolism; Escherichia coli Proteins; Hydrolysis; Immunoblotting; Models, Molecular; Molecular Sequence Data; Mutation; Plasmids/metabolism; Promoter Regions, Genetic; Protein Binding; Protein Conformation; Protein Structure, Tertiary; RNA Polymerase Sigma 54; Sigma Factor/metabolism; Trans-Activators/chemistry; Trans-Activators/metabolism; Transcription, Genetic; Transcriptional Activation; beta-Galactosidase/metabolism |
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