Literature DB >> 23416301

DksA2, a zinc-independent structural analog of the transcription factor DksA.

Ran Furman1, Tapan Biswas, Eric M Danhart, Mark P Foster, Oleg V Tsodikov, Irina Artsimovitch.   

Abstract

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.
Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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Year:  2013        PMID: 23416301      PMCID: PMC5525025          DOI: 10.1016/j.febslet.2013.01.073

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  27 in total

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Journal:  Cell       Date:  2004-08-06       Impact factor: 41.582

2.  Regulation through the secondary channel--structural framework for ppGpp-DksA synergism during transcription.

Authors:  Anna Perederina; Vladimir Svetlov; Marina N Vassylyeva; Tahir H Tahirov; Shigeyuki Yokoyama; Irina Artsimovitch; Dmitry G Vassylyev
Journal:  Cell       Date:  2004-08-06       Impact factor: 41.582

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Authors:  Rosa E Hansen; Jakob R Winther
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4.  Escherichia coli DksA binds to Free RNA polymerase with higher affinity than to RNA polymerase in an open complex.

Authors:  Christopher W Lennon; Tamas Gaal; Wilma Ross; Richard L Gourse
Journal:  J Bacteriol       Date:  2009-07-17       Impact factor: 3.490

Review 5.  Time-resolved fluorescence of proteins.

Authors:  J M Beechem; L Brand
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6.  An insertion in the catalytic trigger loop gates the secondary channel of RNA polymerase.

Authors:  Ran Furman; Oleg V Tsodikov; Yuri I Wolf; Irina Artsimovitch
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Authors:  Karl Perron; Rachel Comte; Christian van Delden
Journal:  Mol Microbiol       Date:  2005-05       Impact factor: 3.501

8.  Role of native disulfide bonds in the structure and activity of insulin-like growth factor 1: genetic models of protein-folding intermediates.

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Authors:  Alexa Price-Whelan; Lars E P Dietrich; Dianne K Newman
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  15 in total

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2.  Characterization of a novel RNA polymerase mutant that alters DksA activity.

Authors:  Dominik Satory; Jennifer A Halliday; Priya Sivaramakrishnan; Rhonald C Lua; Christophe Herman
Journal:  J Bacteriol       Date:  2013-07-12       Impact factor: 3.490

3.  Puzzling conformational changes affecting proteins binding to the RNA polymerase.

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Authors:  Calvin A Henard; Timothy Tapscott; Matthew A Crawford; Maroof Husain; Paschalis-Thomas Doulias; Steffen Porwollik; Lin Liu; Michael McClelland; Harry Ischiropoulos; Andrés Vázquez-Torres
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5.  The Pseudomonas aeruginosa DksA1 protein is involved in H2O2 tolerance and within-macrophages survival and can be replaced by DksA2.

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6.  Systematic identification of molecular mediators of interspecies sensing in a community of two frequently coinfecting bacterial pathogens.

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7.  The Small RNAs PA2952.1 and PrrH as Regulators of Virulence, Motility, and Iron Metabolism in Pseudomonas aeruginosa.

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8.  Contributions of Sinorhizobium meliloti Transcriptional Regulator DksA to Bacterial Growth and Efficient Symbiosis with Medicago sativa.

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9.  The DnaK/DnaJ Chaperone System Enables RNA Polymerase-DksA Complex Formation in Salmonella Experiencing Oxidative Stress.

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10.  pH dependence of the stress regulator DksA.

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