The dimeric form of the unphosphorylated response regulator BaeR

Protein Science

Volumn 22, Issue 9, 2013, Pages 1287-1293

  Choudhury, Hassanul G ^a,b,c   Beis, Konstantinos ^a,b,c  

^a IMPERIAL COLLEGE LONDON   (United Kingdom)

^b Harwell Science and Innovation Campus   (United Kingdom)

^c Oxford Protein Production Facility UK   (United Kingdom)

Author keywords

Asymmetric dimer; Domain swap receiver domain; Effector domain; Unphosphorylated response regulator

Indexed keywords

BACTERIAL PROTEIN; DIMER; HOLMIUM; RESPONSE REGULATOR BAER; SELENOMETHIONINE; TANTALUM; UNCLASSIFIED DRUG; BAER PROTEIN, E COLI; ESCHERICHIA COLI PROTEIN; PHOP PROTEIN, BACTERIA; TRANSACTIVATOR PROTEIN;

ARTICLE; BACTERIAL PHENOMENA AND FUNCTIONS; CRYSTAL STRUCTURE; DIFFRACTION; ESCHERICHIA COLI; HYDROGEN BOND; MOLECULE; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PHOSPHORYLATION; PLASTICITY; PRIORITY JOURNAL; TRANSACTIVATION; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; METABOLISM; MOLECULAR CLONING; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION;

BACTERIAL PROTEINS; CLONING, MOLECULAR; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MODELS, MOLECULAR; MYCOBACTERIUM TUBERCULOSIS; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; TRANS-ACTIVATORS;

EID: 84892944465     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2311     Document Type: Article

References (33)

1. Lomovskaya O, Lewis K, Matin A (1995) EmrR is a negative regulator of the Escherichia coli multidrug resistance pump EmrAB. J Bacteriol 177:2328-2334.
2. Ma D, Alberti M, Lynch C, Nikaido H, Hearst JE (1996) The local repressor AcrR plays a modulating role in the regulation of acrAB genes of Escherichia coli by global stress signals. Mol Microbiol 19:101-112.
3. Okusu H, Ma D, Nikaido H (1996) AcrAB efflux pump plays a major role in the antibiotic resistance phenotype of Escherichia coli multiple-antibiotic- resistance (Mar) mutants. J Bacteriol 178:306-308.
4. Tanaka T, Horii T, Shibayama K, Sato K, Ohsuka S, Arakawa Y, Yamaki K, Takagi K, Ohta M (1997) RobAinduced multiple antibiotic resistance largely depends on the activation of the AcrAB efflux. Microbiol Immunol 41:697-702.
5. White DG, Goldman JD, Demple B, Levy SB (1997) Role of the acrAB locus in organic solvent tolerance mediated by expression of marA, soxS, or robA in Escherichia coli. J Bacteriol 179:6122-6126.
6. Xiong A, Gottman A, Park C, Baetens M, Pandza S, Matin A (2000) The EmrR protein represses the Escherichia coli emrRAB multidrug resistance operon by directly binding to its promoter region. Antimicrob Agents Chemother 44:2905-2907.
7. Stock AM, Robinson VL, Goudreau PN (2000) Two-component signal transduction. Annu Rev Biochem 69: 183-215.
8. Nagakubo S, Nishino K, Hirata T, Yamaguchi A (2002) The putative response regulator BaeR stimulates multidrug resistance of Escherichia coli via a novel multidrug exporter system, MdtABC. J Bacteriol 184:4161- 4167.
9. Leblanc SK, Oates CW, Raivio TL (2011) Characterization of the induction and cellular role of the BaeSR two-component envelope stress response of Escherichia coli. J Bacteriol 193:3367-3375.
10. Baranova N, Nikaido H (2002) The baeSR twocomponent regulatory system activates transcription of the yegMNOB (mdtABCD) transporter gene cluster in Escherichia coli and increases its resistance to novobiocin and deoxycholate. J Bacteriol 184:4168-4176.
11. Hirakawa H, Inazumi Y, Masaki T, Hirata T, Yamaguchi A (2005) Indole induces the expression of multidrug exporter genes in Escherichia coli. Mol Microbiol 55:1113-1126.
12. Appia-Ayme C, Patrick EJ, Sullivan M, Alston MJ, Field SJ, Abuoun M, Anjum MF, Rowley G (2011) Novel inducers of the envelope stress response BaeSR in Salmonella typhimurium: BaeR is critically required for tungstate waste disposal. PLoS One 6:e23713.
13. Nishino K, Nikaido E, Yamaguchi A (2007) Regulation of multidrug efflux systems involved in multidrug and metal resistance of Salmonella enterica serovar Typhimurium. J Bacteriol 189:9066-9075.
14. Hu WS, Chen HW, Zhang RY, Huang CY, Shen CF (2011) The expression levels of outer membrane proteins STM1530 and OmpD, which are influenced by the CpxAR and BaeSR two-component systems, play important roles in the ceftriaxone resistance of Salmonella enterica serovar Typhimurium. Antimicrob Agents Chemother 55:3829-3837.
15. Yamamoto K, Ogasawara H, Ishihama A (2008) Involvement of multiple transcription factors for metalinduced spy gene expression in Escherichia coli. J Biotechnol 133:196-200.
16. Martinez-Hackert E, Stock AM (1997) Structural relationships in the OmpR family of winged-helix transcription factors. J Mol Biol 269:301-312.
17. Buckler DR, Zhou Y, Stock AM (2002) Evidence of intradomain and interdomain flexibility in an OmpR/PhoB homolog from Thermotoga maritima. Structure 10:153-164.
18. Robinson VL, Wu T, Stock AM (2003) Structural analysis of the domain interface in DrrB, a response regulator of the OmpR/PhoB subfamily. J Bacteriol 185:4186- 4194.
19. Nowak E, Panjikar S, Konarev P, Svergun DI, Tucker PA (2006) The structural basis of signal transduction for the response regulator PrrA from Mycobacterium tuberculosis. J Biol Chem 281:9659-9666.
20. Friedland N, Mack TR, Yu M, Hung LW, Terwilliger TC, Waldo GS, Stock AM (2007) Domain orientation in the inactive response regulator Mycobacterium tuberculosis MtrA provides a barrier to activation. Biochemistry 46:6733-6743.
21. King-Scott J, Nowak E, Mylonas E, Panjikar S, Roessle M, Svergun DI, Tucker PA (2007) The structure of a full-length response regulator from Mycobacterium tuberculosis in a stabilized three-dimensional domainswapped, activated state. J Biol Chem 282:37717- 37729.
22. Menon S, Wang S (2011) Structure of the response regulator PhoP from Mycobacterium tuberculosis reveals a dimer through the receiver domain. Biochemistry 50: 5948-5957.
23. Bachhawat P, Swapna GV, Montelione GT, Stock AM (2005) Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active states. Structure 13:1353-1363.
24. Toro-Roman A, Wu T, Stock AM (2005) A common dimerization interface in bacterial response regulators KdpE and TorR. Protein Sci 14:3077-3088.
25. Gao R, Stock AM (2010) Molecular strategies for phosphorylation-mediated regulation of response regulator activity. Curr Opin Microbiol 13:160-167.
26. Milani M, Leoni L, Rampioni G, Zennaro E, Ascenzi P, Bolognesi M (2005) An active-like structure in the unphosphorylated StyR response regulator suggests a phosphorylation-dependent allosteric activation mechanism. Structure 13:1289-1297.
27. Blanco AG, Sola M, Gomis-Ruth FX, Coll M (2002) Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 10:701-713.
28. Rhee JE, Sheng W, Morgan LK, Nolet R, Liao X, Kenney LJ (2008) Amino acids important for DNA recognition by the response regulator OmpR. J Biol Chem 283:8664-8677.
29. Winter G (2010) xia2: An expert system for macromolecular crystallography data reduction. J Appl Cryst 43:186-190.
30. Sheldrick GM (2008) A short history of SHELX. Acta Cryst A64:112-122.
31. Vonrhein C, Blanc E, Roversi P, Bricogne G (2007) Automated structure solution with autoSHARP. Methods Mol Biol 364:215-230.
32. McCoy AJ, Grosse-Kunstleve RW, Adams PD, Winn MD, Storoni LC, Read RJ (2007) Phaser crystallographic software. J Appl Cryst 40:658-674.
33. Adams PD, Afonine PV, Bunkoeczi G, Chen VB, Davis IW, Echols N, Headd JJ, Hung LW, Kapral GJ, Grosse- Kunstleve RW, McCoy AJ, Moriarty NW, Oeffner R, Read RJ, Richardson DC, Richardson JS, Terwilliger TC, Zwart PH (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Cryst D 66:213-221.