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Investigating protein–protein interfaces in bacterial transcription complexes: a fragmentation approach
Author(s) -
Burrows Patricia C.
Publication year - 2003
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.10388
Subject(s) - transcription (linguistics) , atp hydrolysis , rna polymerase , superfamily , microbiology and biotechnology , biology , polymerase , computational biology , atpase , biophysics , transcription factor , genetics , rna , biochemistry , enzyme , gene , philosophy , linguistics
Transcription initiation by σ 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 σ 54 ‐dependent transcriptional activators that constitutes a σ 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. BioEssays 25:1150–1153, 2003. © 2003 Wiley Periodicals, Inc.