Two-component systems of Mycobacterium tuberculosis: structure-based approaches.

Mycobacterium tuberculosis contains few two-component systems compared to many other bacteria, possibly because it has more serine/threonine signaling pathways. Even so, these two-component systems appear to play an important role in early intracellular survival of the pathogen as well as in aspects of virulence. In this chapter, we discuss what has been learned about the mycobacterial two-component systems, with particular emphasis on knowledge gained from structural genomics projects.

[1]  A Keith Dunker,et al.  Order, disorder, and flexibility: prediction from protein sequence. , 2003, Structure.

[2]  J. Tyagi,et al.  Signal transduction systems of mycobacteria with special reference to M. tuberculosis , 2004 .

[3]  Irina Kolesnikova,et al.  The Mycobacterium tuberculosis PhoPR two‐component system regulates genes essential for virulence and complex lipid biosynthesis , 2006, Molecular microbiology.

[4]  B. Gicquel,et al.  An essential role for phoP in Mycobacterium tuberculosis virulence , 2001, Molecular microbiology.

[5]  Dmitri I. Svergun,et al.  New developments in direct shape determination from small-angle scattering. 2. Uniqueness , 1996 .

[6]  T. Kawamoto,et al.  DNA binding of PhoB and its interaction with RNA polymerase. , 1996, Journal of molecular biology.

[7]  V. Deretic,et al.  An Essential Two-Component Signal Transduction System in Mycobacterium tuberculosis , 2000, Journal of bacteriology.

[8]  Victor S Lamzin,et al.  Auto-rickshaw: an automated crystal structure determination platform as an efficient tool for the validation of an X-ray diffraction experiment. , 2005, Acta crystallographica. Section D, Biological crystallography.

[9]  W. Benjamin,et al.  Expression, Autoregulation, and DNA Binding Properties of the Mycobacterium tuberculosis TrcR Response Regulator , 2002, Journal of bacteriology.

[10]  E. Rubin,et al.  Comprehensive identification of conditionally essential genes in mycobacteria , 2001, Proceedings of the National Academy of Sciences of the United States of America.

[11]  W. Jacobs,et al.  Molecular genetics of mycobacteria. , 2000 .

[12]  S. Haydel,et al.  Global expression analysis of two-component system regulator genes during Mycobacterium tuberculosis growth in human macrophages. , 2004, FEMS microbiology letters.

[13]  D I Svergun,et al.  Determination of domain structure of proteins from X-ray solution scattering. , 2001, Biophysical journal.

[14]  Dmitri I Svergun,et al.  Global rigid body modeling of macromolecular complexes against small-angle scattering data. , 2005, Biophysical journal.

[15]  F. Tarendeau,et al.  Combinatorial library approaches for improving soluble protein expression in Escherichia coli. , 2006, Acta crystallographica. Section D, Biological crystallography.

[16]  Ann M Stock,et al.  Evidence of intradomain and interdomain flexibility in an OmpR/PhoB homolog from Thermotoga maritima. , 2002, Structure.

[17]  Dirk Schnappinger,et al.  Inhibition of Respiration by Nitric Oxide Induces a Mycobacterium tuberculosis Dormancy Program , 2003, The Journal of experimental medicine.

[18]  D Spruce,et al.  Automation of the collection and processing of X-ray diffraction data -- a generic approach. , 2002, Acta crystallographica. Section D, Biological crystallography.

[19]  T. N. Bhat,et al.  The Protein Data Bank , 2000, Nucleic Acids Res..

[20]  E. Rubin,et al.  Genes required for mycobacterial growth defined by high density mutagenesis , 2003, Molecular microbiology.

[21]  W. Hendrickson.  Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. , 1991, Science.

[22]  V. Deretic,et al.  Mycobacterium tuberculosis signal transduction system required for persistent infections , 2001, Proceedings of the National Academy of Sciences of the United States of America.

[23]  B. Barrell,et al.  Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence , 1998, Nature.

[24]  D. Svergun,et al.  Small-angle scattering studies of biological macromolecules in solution , 2003 .

[25]  W. Benjamin,et al.  In vitro evidence of two-component system phosphorylation between the Mycobacterium tuberculosis TrcR/TrcS proteins. , 1999, Microbial pathogenesis.

[26]  D. Sherman,et al.  Structures of Mycobacterium tuberculosis DosR and DosR-DNA complex involved in gene activation during adaptation to hypoxic latency. , 2005, Journal of molecular biology.

[27]  D. Saini,et al.  Cross talk between DevS sensor kinase homologue, Rv2027c, and DevR response regulator of Mycobacterium tuberculosis , 2004, FEBS letters.

[28]  H. Sugimoto,et al.  The signaling pathway in histidine kinase and the response regulator complex revealed by X-ray crystallography and solution scattering. , 2006, Journal of molecular biology.

[29]  Martin Tompa,et al.  Rv3133c/dosR is a transcription factor that mediates the hypoxic response of Mycobacterium tuberculosis , 2003, Molecular microbiology.

[30]  D. Sherman,et al.  Two Sensor Kinases Contribute to the Hypoxic Response of Mycobacterium tuberculosis* , 2004, Journal of Biological Chemistry.

[31]  Sébastien Rodrigue,et al.  σ Factors and Global Gene Regulation in Mycobacterium tuberculosis , 2004, Journal of bacteriology.

[32]  Raymond L. Hovey,et al.  MprAB Is a Stress-Responsive Two-Component System That Directly Regulates Expression of Sigma Factors SigB and SigE in Mycobacterium tuberculosis , 2006, Journal of bacteriology.

[33]  L Wernisch,et al.  The Mycobacterium tuberculosis dosRS two-component system is induced by multiple stresses. , 2004, Tuberculosis.

[34]  D. Svergun,et al.  CRYSOL : a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates , 1995 .

[35]  D I Svergun,et al.  Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. , 1999, Biophysical journal.

[36]  D. Saini,et al.  Disruption of response regulator gene, devR, leads to attenuation in virulence of Mycobacterium tuberculosis. , 2004, FEMS microbiology letters.

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

[38]  David Eisenberg,et al.  Structural genomics of Mycobacterium tuberculosis: a preliminary report of progress at UCLA. , 2003, Biophysical chemistry.

[39]  A. Das,et al.  Functional insights from the molecular modelling of a novel two-component system. , 2006, Biochemical and biophysical research communications.

[40]  D. Saini,et al.  DevR-DevS is a bona fide two-component system of Mycobacterium tuberculosis that is hypoxia-responsive in the absence of the DNA-binding domain of DevR. , 2004, Microbiology.

[41]  Wayne A Hendrickson,et al.  Structure of the entire cytoplasmic portion of a sensor histidine‐kinase protein , 2005, The EMBO journal.

[42]  L. Pearl,et al.  Crystal structure and induction mechanism of AmiC–AmiR: a ligand‐regulated transcription antitermination complex , 1999, The EMBO journal.

[43]  Gurdyal S Besra,et al.  Mycolic acid biosynthesis and enzymic characterization of the beta-ketoacyl-ACP synthase A-condensing enzyme from Mycobacterium tuberculosis. , 2002, The Biochemical journal.

[44]  Thomas L. Madden,et al.  Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. , 1997, Nucleic acids research.

[45]  Christian von Mering,et al.  STRING: a database of predicted functional associations between proteins , 2003, Nucleic Acids Res..

[46]  J. Saldanha,et al.  A two-component signal transduction system with a PAS domain-containing sensor is required for virulence of Mycobacterium tuberculosis in mice. , 2004, Biochemical and biophysical research communications.

[47]  P. Tucker,et al.  A novel two‐component system found in Mycobacterium tuberculosis , 2005, FEBS letters.

[48]  Michael Y. Galperin.  Structural Classification of Bacterial Response Regulators: Diversity of Output Domains and Domain Combinations , 2006, Journal of bacteriology.

[49]  L. J. Perry,et al.  The crystal and solution structure of a putative transcriptional antiterminator from Mycobacterium tuberculosis. , 2004, Structure.

[50]  D. Svergun,et al.  Insights into signal transduction revealed by the low resolution structure of the FixJ response regulator. , 2002, Journal of molecular biology.

[51]  Tanya Parish,et al.  The senX3-regX3 two-component regulatory system of Mycobacterium tuberculosis is required for virulence. , 2003, Microbiology.

[52]  C. Locht,et al.  Intracellular autoregulation of the Mycobacterium tuberculosis PrrA response regulator. , 2004, Microbiology.

[53]  M. Solà,et al.  Tandem DNA Recognition by Two-Component Signal Transduction Transcriptional Activator Phob , 2002 .

[54]  S. Haydel,et al.  The Mycobacterium tuberculosis TrcR Response Regulator Represses Transcription of the Intracellularly Expressed Rv1057 Gene, Encoding a Seven-Bladed β-Propeller , 2006, Journal of bacteriology.

[55]  Tanya Parish,et al.  Deletion of Two-Component Regulatory Systems Increases the Virulence of Mycobacterium tuberculosis , 2003, Infection and Immunity.

[56]  Peter V. Konarev,et al.  MASSHA – a graphics system for rigid-body modelling of macromolecular complexes against solution scattering data , 2001 .

[57]  W. Jacobs,et al.  The effects of reactive nitrogen intermediates on gene expression in Mycobacterium tuberculosis , 2003, Cellular microbiology.

[58]  M. Solà,et al.  Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. , 2002, Structure.

[59]  Dmitri I. Svergun,et al.  PRIMUS: a Windows PC-based system for small-angle scattering data analysis , 2003 .

[60]  C. Locht,et al.  Molecular characterization of the mycobacterial SenX3-RegX3 two-component system: evidence for autoregulation. , 2000, Microbiology.

[61]  P. Nordlund,et al.  Colony filtration blotting for screening soluble expression in Escherichia coli , 2006, Nature Protocols.

[62]  C. Locht,et al.  Transient Requirement of the PrrA-PrrB Two-Component System for Early Intracellular Multiplication of Mycobacterium tuberculosis , 2002, Infection and Immunity.

[63]  Christopher E. Wozniak,et al.  Functional Analysis of theMycobacterium tuberculosis MprAB Two-Component SignalTransductionSystem , 2003, Infection and Immunity.

[64]  Ann M Stock,et al.  Structural Analysis of the Domain Interface in DrrB, a Response Regulator of the OmpR/PhoB Subfamily , 2003, Journal of bacteriology.

[65]  L. J. Perry,et al.  Protein production in Escherichia coli for structural studies by X-ray crystallography. , 2003, Journal of structural biology.

[66]  Christopher M. Sassetti,et al.  Genetic requirements for mycobacterial survival during infection , 2003, Proceedings of the National Academy of Sciences of the United States of America.

[67]  C P Ponting,et al.  The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins. , 1999, FEMS microbiology letters.

[68]  V. Stewart,et al.  Probing Conservation of HAMP Linker Structure and Signal Transduction Mechanism through Analysis of Hybrid Sensor Kinases , 2003, Journal of bacteriology.

[69]  Maxim V. Petoukhov,et al.  ATSAS 2.1, a program package for small‐angle scattering data analysis , 2006 .

[70]  Brigitte Gicquel,et al.  The Virulence-associated Two-component PhoP-PhoR System Controls the Biosynthesis of Polyketide-derived Lipids in Mycobacterium tuberculosis* , 2006, Journal of Biological Chemistry.

[71]  P. Tucker,et al.  Structural and functional aspects of the sensor histidine kinase PrrB from Mycobacterium tuberculosis. , 2006, Structure.

[72]  Robert B. Russell,et al.  GlobPlot: exploring protein sequences for globularity and disorder , 2003, Nucleic Acids Res..

[73]  Dirk Schnappinger,et al.  Regulation of the Mycobacterium tuberculosis hypoxic response gene encoding α-crystallin , 2001, Proceedings of the National Academy of Sciences of the United States of America.

[74]  T. Mizuno.  Two-Component Phosphorelay Signal Transduction Systems in Plants: from Hormone Responses to Circadian Rhythms , 2005, Bioscience, biotechnology, and biochemistry.