Investigating protein-protein interfaces in bacterial transcription complexes: a fragmentation approach.
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.
Burrows
Patricia C
PC
Department of Biological Sciences, Sir Alexander Fleming Building Imperial College London, South Kensington Campus, London SW7 2AZ. patricia.c.burrows@imperial.ac.uk
D000255:Adenosine Triphosphate / Q000737:chemistry; D020816:Amino Acid Motifs; D018407:Bacterial Physiological Phenomena; D001665:Binding Sites; D004268:DNA-Binding Proteins; D012321:DNA-Directed RNA Polymerases / Q000737:chemistry / Q000502:physiology*; D004926:Escherichia coli / Q000502:physiology; D029968:Escherichia coli Proteins; D006868:Hydrolysis; D008954:Models, Biological; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D051877:RNA Polymerase Sigma 54; D012808:Sigma Factor / Q000737:chemistry; D014157:Transcription Factors / Q000378:metabolism; D014158:Transcription, Genetic; D015533:Transcriptional Activation
D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D012808:Sigma Factor; D014157:Transcription Factors; C497751:rpoN protein, E coli; D000255:Adenosine Triphosphate; D012321:DNA-Directed RNA Polymerases; D051877:RNA Polymerase Sigma 54