Regulatory mechanisms of thiol-based redox sensors: lessons learned from structural studies on prokaryotic redox sensors

[1]  N. Ketheesan,et al.  Redox-sensitive transcription factors play a significant role in the development of rheumatoid arthritis , 2018, International reviews of immunology.

[2]  A. Price-Whelan,et al.  Redox-Based Regulation of Bacterial Development and Behavior. , 2017, Annual review of biochemistry.

[3]  Frédéric Barras,et al.  Oxidative stress, protein damage and repair in bacteria , 2017, Nature Reviews Microbiology.

[4]  S. Choi,et al.  The hydrogen peroxide hypersensitivity of OxyR2 in Vibrio vulnificus depends on conformational constraints , 2017, The Journal of Biological Chemistry.

[5]  Michelle L. Reniere,et al.  A Redox-Responsive Transcription Factor Is Critical for Pathogenesis and Aerobic Growth of Listeria monocytogenes , 2017, Infection and Immunity.

[6]  J. Gan,et al.  Structural Analysis of the Hg(II)-Regulatory Protein Tn501 MerR from Pseudomonas aeruginosa , 2016, Scientific Reports.

[7]  H. Yoon,et al.  Two distinct mechanisms of transcriptional regulation by the redox sensor YodB , 2016, Proceedings of the National Academy of Sciences.

[8]  R. Couñago,et al.  Structural basis of thiol-based regulation of formaldehyde detoxification in H. influenzae by a MerR regulator with no sensor region , 2016, Nucleic acids research.

[9]  F. Fang,et al.  Redox-Active Sensing by Bacterial DksA Transcription Factors Is Determined by Cysteine and Zinc Content , 2016, mBio.

[10]  Zhaohui Xu,et al.  Does the Transcription Factor NemR Use a Regulatory Sulfenamide Bond to Sense Bleach? , 2015, Antioxidants & redox signaling.

[11]  Ilyas Yildirim,et al.  Allosteric transcriptional regulation via changes in the overall topology of the core promoter , 2015, Science.

[12]  Chieh-Chen Huang,et al.  Structural basis of the mercury(II)-mediated conformational switching of the dual-function transcriptional regulator MerR , 2015, Nucleic acids research.

[13]  H. Antelmann,et al.  Thiol-based redox switches in prokaryotes , 2015, Biological chemistry.

[14]  Inseong Jo,et al.  Structural details of the OxyR peroxide-sensing mechanism , 2015, Proceedings of the National Academy of Sciences.

[15]  Vu Van Loi,et al.  Redox regulation by reversible protein S-thiolation in bacteria , 2015, Front. Microbiol..

[16]  H. Wright,et al.  Structures of the Porphyromonas gingivalis OxyR regulatory domain explain differences in expression of the OxyR regulon in Escherichia coli and P. gingivalis. , 2013, Acta crystallographica. Section D, Biological crystallography.

[17]  Ursula Jakob,et al.  The RclR Protein Is a Reactive Chlorine-specific Transcription Factor in Escherichia coli * , 2013, The Journal of Biological Chemistry.

[18]  Ursula Jakob,et al.  Bacterial responses to reactive chlorine species. , 2013, Annual review of microbiology.

[19]  J. Imlay,et al.  The molecular mechanisms and physiological consequences of oxidative stress: lessons from a model bacterium , 2013, Nature Reviews Microbiology.

[20]  S. Peterson,et al.  Molecular mechanism of quinone signaling mediated through S-quinonization of a YodB family repressor QsrR , 2013, Proceedings of the National Academy of Sciences of the United States of America.

[21]  Michael T Laub,et al.  Evolution of two-component signal transduction systems. , 2012, Annual review of microbiology.

[22]  U. Förstermann,et al.  Nitric oxide synthases: regulation and function. , 2012, European heart journal.

[23]  R. Read,et al.  Structural insights into the redox-switch mechanism of the MarR/DUF24-type regulator HypR , 2012, Nucleic acids research.

[24]  D. Ortiz de Orué Lucana,et al.  ROS-Mediated Signalling in Bacteria: Zinc-Containing Cys-X-X-Cys Redox Centres and Iron-Based Oxidative Stress , 2011, Journal of signal transduction.

[25]  J. Helmann,et al.  Thiol-based redox switches and gene regulation. , 2011, Antioxidants & redox signaling.

[26]  M. Hecker,et al.  The redox‐sensing regulator YodB senses quinones and diamide via a thiol‐disulfide switch in Bacillus subtilis , 2010, Proteomics.

[27]  Cai-Guang Yang,et al.  Structural insight into the oxidation‐sensing mechanism of the antibiotic resistance of regulator MexR , 2010, EMBO reports.

[28]  S. Sainsbury,et al.  The structure of a reduced form of OxyR from Neisseria meningitidis , 2010, BMC Structural Biology.

[29]  R. Brennan,et al.  Promoter Recognition by a Complex of Spx and the C-Terminal Domain of the RNA Polymerase α Subunit , 2010, PloS one.

[30]  V. Lamour,et al.  Crystal structure of the in vivo-assembled Bacillus subtilis Spx/RNA polymerase alpha subunit C-terminal domain complex. , 2009, Journal of structural biology.

[31]  B. Freeman,et al.  Transduction of Redox Signaling by Electrophile-Protein Reactions , 2009, Science Signaling.

[32]  J. Imlay.  Cellular defenses against superoxide and hydrogen peroxide. , 2008, Annual review of biochemistry.

[33]  K. Miki,et al.  Crystal structure of the [2Fe-2S] oxidative-stress sensor SoxR bound to DNA , 2008, Proceedings of the National Academy of Sciences.

[34]  R. Brennan,et al.  Structural mechanism of organic hydroperoxide induction of the transcription regulator OhrR. , 2007, Molecular cell.

[35]  Kazuo Kobayashi,et al.  Dual Negative Control of spx Transcription Initiation from the P3 Promoter by Repressors PerR and YodB in Bacillus subtilis , 2006, Journal of bacteriology.

[36]  P. Tucker,et al.  The Structural Basis of Signal Transduction for the Response Regulator PrrA from Mycobacterium tuberculosis* , 2006, Journal of Biological Chemistry.

[37]  R. Brennan,et al.  Crystal structure of the Bacillus subtilis anti-alpha, global transcriptional regulator, Spx, in complex with the alpha C-terminal domain of RNA polymerase. , 2005, Proceedings of the National Academy of Sciences of the United States of America.

[38]  R. Brennan,et al.  Structure of an OhrR-ohrA operator complex reveals the DNA binding mechanism of the MarR family. , 2005, Molecular cell.

[39]  D. Pignol,et al.  PpsR: a multifaceted regulator of photosynthesis gene expression in purple bacteria , 2005, Molecular microbiology.

[40]  Jeffrey Green,et al.  Bacterial redox sensors , 2004, Nature Reviews Microbiology.

[41]  D. Barford.  The role of cysteine residues as redox-sensitive regulatory switches. , 2004, Current opinion in structural biology.

[42]  G. Storz,et al.  Redox regulation of OxyR requires specific disulfide bond formation involving a rapid kinetic reaction path , 2004, Nature Structural &Molecular Biology.

[43]  C. Bauer,et al.  RegB/RegA, a Highly Conserved Redox-Responding Global Two-Component Regulatory System , 2004, Microbiology and Molecular Biology Reviews.

[44]  R. Brennan,et al.  The Structural Mechanism for Transcription Activation by MerR Family Member Multidrug Transporter Activation, N Terminus* , 2004, Journal of Biological Chemistry.

[45]  P. Zuber.  Spx-RNA Polymerase Interaction and Global Transcriptional Control during Oxidative Stress , 2004, Journal of bacteriology.

[46]  G. Storz,et al.  Prominent roles of the NorR and Fur regulators in the Escherichia coli transcriptional response to reactive nitrogen species. , 2004, Proceedings of the National Academy of Sciences of the United States of America.

[47]  M. Williamson,et al.  Solution structure and DNA binding of the effector domain from the global regulator PrrA (RegA) from Rhodobacter sphaeroides: insights into DNA binding specificity. , 2003, Nucleic acids research.

[48]  A. Mondragón,et al.  Molecular Basis of Metal-Ion Selectivity and Zeptomolar Sensitivity by CueR , 2003, Science.

[49]  C. Jacob,et al.  Multiple roles of cysteine in biocatalysis. , 2003, Biochemical and biophysical research communications.

[50]  J. Helmann,et al.  The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[51]  C. Bauer,et al.  Repression of photosynthesis gene expression by formation of a disulfide bond in CrtJ , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[52]  J. Imlay,et al.  Hydrogen Peroxide Fluxes and Compartmentalization inside Growing Escherichia coli , 2001, Journal of bacteriology.

[53]  S. Mongkolsuk,et al.  Complex Regulation of the Organic Hydroperoxide Resistance Gene (ohr) from XanthomonasInvolves OhrR, a Novel Organic Peroxide-Inducible Negative Regulator, and Posttranscriptional Modifications , 2001, Journal of bacteriology.

[54]  Thomas D. Schneider,et al.  Computation-Directed Identification of OxyR DNA Binding Sites in Escherichia coli , 2001, Journal of bacteriology.

[55]  J. Helmann,et al.  OhrR Is a Repressor of ohrA, a Key Organic Hydroperoxide Resistance Determinant in Bacillus subtilis , 2001, Journal of bacteriology.

[56]  G. Storz,et al.  Structural Basis of the Redox Switch in the OxyR Transcription Factor , 2001, Cell.

[57]  R. Brennan,et al.  Crystal structure of the transcription activator BmrR bound to DNA and a drug , 2001, Nature.

[58]  E. Cabiscol,et al.  Oxidative stress in bacteria and protein damage by reactive oxygen species. , 2000, International microbiology : the official journal of the Spanish Society for Microbiology.

[59]  G. Storz,et al.  Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[60]  L. Szweda,et al.  Selective inactivation of alpha-ketoglutarate dehydrogenase and pyruvate dehydrogenase: reaction of lipoic acid with 4-hydroxy-2-nonenal. , 1998, Biochemistry.

[61]  G. Storz,et al.  Activation of the OxyR transcription factor by reversible disulfide bond formation. , 1998, Science.

[62]  C. Nathan,et al.  Regulation of biosynthesis of nitric oxide. , 1994, The Journal of biological chemistry.

[63]  R. Soberman,et al.  Specificity of a third kind : reactive oxygen and nitrogen intermediates in cell signaling , 2022 .