Publikationsdatum:
2013-03-13
Beschreibung:
The relative levels of different factors dictate the expression profile of a bacterium. Extracytoplasmic function factors synchronize the transcriptional profile with environmental conditions. The cellular concentration of free extracytoplasmic function factors is regulated by the localization of this protein in a /anti- complex. Anti- factors are multi-domain proteins with a receptor to sense environmental stimuli and a conserved anti- domain (ASD) that binds a factor. Here we describe the structure of Mycobacterium tuberculosis anti- D (RsdA) in complex with the -35 promoter binding domain of D ( D 4 ). We note distinct conformational features that enable the release of D by the selective proteolysis of the ASD in RsdA. The structural and biochemical features of the D /RsdA complex provide a basis to reconcile diverse regulatory mechanisms that govern /anti- interactions despite high overall structural similarity. Multiple regulatory mechanisms embedded in an ASD scaffold thus provide an elegant route to rapidly re-engineer the expression profile of a bacterium in response to an environmental stimulus.
Print ISSN:
0305-1048
Digitale ISSN:
1362-4962
Thema:
Biologie
