PMID:14635249

Citation	Burrows, PC (2003) Investigating protein-protein interfaces in bacterial transcription complexes: a fragmentation approach. Bioessays 25:1150-3
Abstract	Transcription initiation by sigma(54)-RNA polymerase (RNAP) relies explicitly on a transient interaction with a complex molecular machine belonging to the AAA+ (ATPases associated with various cellular activities) superfamily. Members of the AAA+ superfamily convert chemical energy derived from NTP hydrolysis to a mechanical force used to remodel their target substrate. Recently Bordes and colleagues,1 using a protein fragmentation approach, identified a unique sequence within sigma(54)-dependent transcriptional activators that constitutes a sigma(54)-binding interface. This interface is not static, but subject to nucleotide-dependent movement which may represent a common mechanism for controlling output that has been adopted by other AAA+ proteins.
Links	PubMed Online version:10.1002/bies.10388
Keywords	Adenosine Triphosphate/chemistry; Amino Acid Motifs; Bacterial Physiological Phenomena; Binding Sites; DNA-Binding Proteins; DNA-Directed RNA Polymerases/chemistry; DNA-Directed RNA Polymerases/physiology; Escherichia coli/physiology; Escherichia coli Proteins; Hydrolysis; Models, Biological; Protein Binding; Protein Structure, Tertiary; RNA Polymerase Sigma 54; Sigma Factor/chemistry; Transcription Factors/metabolism; Transcription, Genetic; Transcriptional Activation
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