Structural highlights
Publication Abstract from PubMed
Transcription factor DksA contains a four-Cys Zn(2 +)-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 Zn(2+) limitation. Although DksA2 does not bind Zn(2+), 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).
DksA2, a zinc-independent structural analog of the transcription factor DksA.,Furman R, Biswas T, Danhart EM, Foster MP, Tsodikov OV, Artsimovitch I FEBS Lett. 2013 Feb 14. pii: S0014-5793(13)00123-3. doi:, 10.1016/j.febslet.2013.01.073. PMID:23416301[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Furman R, Biswas T, Danhart EM, Foster MP, Tsodikov OV, Artsimovitch I. DksA2, a zinc-independent structural analog of the transcription factor DksA. FEBS Lett. 2013 Feb 14. pii: S0014-5793(13)00123-3. doi:, 10.1016/j.febslet.2013.01.073. PMID:23416301 doi:http://dx.doi.org/10.1016/j.febslet.2013.01.073
