Abstract
Transcription factor DksA contains a four-Cys Zn2 +-finger motif thought to be responsible for structural integrity and the relative disposition of its domains. Pseudomonas aeruginosa encodes an additional DksA paralog (DksA2) that is expressed selectively under Zn2+ limitation. Although DksA2 does not bind Zn2+, it complements the Escherichia coli dksA deletion and has similar effects on transcription in vitro. In this study, structural and biochemical analyses reveal that DksA2 has a similar fold, domain structure and RNA polymerase binding properties to those of the E. coli DksA despite the lack of the stabilizing metal ion.Structured summary of protein interactions:RNAPandDksA2bindbybiochemical(View interaction)DksAandRNAPbindbybiochemical(View interaction)DksA2andDksA2bindbyX-ray crystallography(View interaction)
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