1t72 › Citations

Crystal structure of the "PhoU-like" phosphate uptake regulator from Aquifex aeolicus.

Oganesyan V, Oganesyan N, Adams PD, Jancarik J, Yokota HA, Kim R, Kim SH
J Bacteriol 187 4238-44 (2005)
Cited: 24 times
EuropePMC logo PMID: 15937186

Abstract

The phoU gene of Aquifex aeolicus encodes a protein called PHOU_AQUAE with sequence similarity to the PhoU protein of Escherichia coli. Despite the fact that there is a large number of family members (more than 300) attributed to almost all known bacteria and despite PHOU_AQUAE's association with the regulation of genes for phosphate metabolism, the nature of its regulatory function is not well understood. Nearly one-half of these PhoU-like proteins, including both PHOU_AQUAE and the one from E. coli, form a subfamily with an apparent dimer structure of two PhoU domains on the basis of their amino acid sequence. The crystal structure of PHOU_AQUAE (a 221-amino-acid protein) reveals two similar coiled-coil PhoU domains, each forming a three-helix bundle. The structures of PHOU_AQUAE proteins from both a soluble fraction and refolded inclusion bodies (at resolutions of 2.8 and 3.2A, respectively) showed no significant differences. The folds of the PhoU domain and Bag domains (for a class of cofactors of the eukaryotic chaperone Hsp70 family) are similar. Accordingly, we propose that gene regulation by PhoU may occur by association of PHOU_AQUAE with the ATPase domain of the histidine kinase PhoR, promoting release of its substrate PhoB. Other proteins that share the PhoU domain fold include the coiled-coil domains of the STAT protein, the ribosome-recycling factor, and structural proteins like spectrin.

Articles - 1t72 mentioned but not cited (1)

  1. Crystal structure of the "PhoU-like" phosphate uptake regulator from Aquifex aeolicus. Oganesyan V, Oganesyan N, Adams PD, Jancarik J, Yokota HA, Kim R, Kim SH. J. Bacteriol. 187 4238-4244 (2005)


Reviews citing this publication (5)

  1. Molecular regulation of antibiotic biosynthesis in streptomyces. Liu G, Chater KF, Chandra G, Niu G, Tan H. Microbiol. Mol. Biol. Rev. 77 112-143 (2013)
  2. The phosphate regulon and bacterial virulence: a regulatory network connecting phosphate homeostasis and pathogenesis. Lamarche MG, Wanner BL, Crépin S, Harel J. FEMS Microbiol. Rev. 32 461-473 (2008)
  3. Global regulation by the seven-component Pi signaling system. Hsieh YJ, Wanner BL. Curr. Opin. Microbiol. 13 198-203 (2010)
  4. Metabolic Regulation of a Bacterial Cell System with Emphasis on Escherichia coli Metabolism. Shimizu K. ISRN Biochem 2013 645983 (2013)
  5. Activation of the PhoPR-Mediated Response to Phosphate Limitation Is Regulated by Wall Teichoic Acid Metabolism in Bacillus subtilis. Devine KM. Front Microbiol 9 2678 (2018)

Articles citing this publication (18)

  1. Two-component PhoB-PhoR regulatory system and ferric uptake regulator sense phosphate and iron to control virulence genes in type III and VI secretion systems of Edwardsiella tarda. Chakraborty S, Sivaraman J, Leung KY, Mok YK. J. Biol. Chem. 286 39417-39430 (2011)
  2. Employment of a promoter-swapping technique shows that PhoU modulates the activity of the PstSCAB2 ABC transporter in Escherichia coli. Rice CD, Pollard JE, Lewis ZT, McCleary WR. Appl. Environ. Microbiol. 75 573-582 (2009)
  3. The PhoU protein from Escherichia coli interacts with PhoR, PstB, and metals to form a phosphate-signaling complex at the membrane. Gardner SG, Johns KD, Tanner R, McCleary WR. J. Bacteriol. 196 1741-1752 (2014)
  4. Ecophysiology of an ammonia-oxidizing archaeon adapted to low-salinity habitats. Mosier AC, Lund MB, Francis CA. Microb. Ecol. 64 955-963 (2012)
  5. Metabolic regulation of Escherichia coli and its phoB and phoR genes knockout mutants under phosphate and nitrogen limitations as well as at acidic condition. Marzan LW, Shimizu K. Microb. Cell Fact. 10 39 (2011)
  6. Glucosylglycerate biosynthesis in the deepest lineage of the Bacteria: characterization of the thermophilic proteins GpgS and GpgP from Persephonella marina. Costa J, Empadinhas N, da Costa MS. J. Bacteriol. 189 1648-1654 (2007)
  7. The X-ray crystal structures of two constitutively active mutants of the Escherichia coli PhoB receiver domain give insights into activation. Arribas-Bosacoma R, Kim SK, Ferrer-Orta C, Blanco AG, Pereira PJ, Gomis-Rüth FX, Wanner BL, Coll M, Solà M. J. Mol. Biol. 366 626-641 (2007)
  8. Exploiting 3D structural templates for detection of metal-binding sites in protein structures. Goyal K, Mande SC. Proteins 70 1206-1218 (2008)
  9. The signaling pathway in histidine kinase and the response regulator complex revealed by X-ray crystallography and solution scattering. Yamada S, Akiyama S, Sugimoto H, Kumita H, Ito K, Fujisawa T, Nakamura H, Shiro Y. J. Mol. Biol. 362 123-139 (2006)
  10. Defining the functional domain of programmed cell death 10 through its interactions with phosphatidylinositol-3,4,5-trisphosphate. Dibble CF, Horst JA, Malone MH, Park K, Temple B, Cheeseman H, Barbaro JR, Johnson GL, Bencharit S. PLoS ONE 5 e11740 (2010)
  11. PhoY2 of mycobacteria is required for metabolic homeostasis and stress response. Wang C, Mao Y, Yu J, Zhu L, Li M, Wang D, Dong D, Liu J, Gao Q. J. Bacteriol. 195 243-252 (2013)
  12. Metatranscriptomic insights on gene expression and regulatory controls in Candidatus Accumulibacter phosphatis. Oyserman BO, Noguera DR, del Rio TG, Tringe SG, McMahon KD. ISME J 10 810-822 (2016)
  13. Physiological Roles of the Dual Phosphate Transporter Systems in Low and High Phosphate Conditions and in Capsule Maintenance of Streptococcus pneumoniae D39. Zheng JJ, Sinha D, Wayne KJ, Winkler ME. Front Cell Infect Microbiol 6 63 (2016)
  14. Overproduction of YjbB reduces the level of polyphosphate in Escherichia coli: a hypothetical role of YjbB in phosphate export and polyphosphate accumulation. Motomura K, Hirota R, Ohnaka N, Okada M, Ikeda T, Morohoshi T, Ohtake H, Kuroda A. FEMS Microbiol. Lett. 320 25-32 (2011)
  15. Transcriptional and preliminary functional analysis of the six genes located in divergence of phoR/phoP in Streptomyces lividans. Darbon E, Martel C, Nowacka A, Pegot S, Moreau PL, Virolle MJ. Appl. Microbiol. Biotechnol. 95 1553-1566 (2012)
  16. Crystal structure of PhoU from Pseudomonas aeruginosa, a negative regulator of the Pho regulon. Lee SJ, Park YS, Kim SJ, Lee BJ, Suh SW. J. Struct. Biol. 188 22-29 (2014)
  17. The Global Regulator PhoU Positively Controls Growth and Butenyl-Spinosyn Biosynthesis in Saccharopolyspora pogona. Tang J, Chen J, Liu Y, Hu J, Xia Z, Li X, He H, Rang J, Sun Y, Yu Z, Cui J, Xia L. Front Microbiol 13 904627 (2022)
  18. Transcriptome analysis of wild-type and afsS deletion mutant strains identifies synergistic transcriptional regulator of afsS for a high antibiotic-producing strain of Streptomyces coelicolor A3(2). Kim MW, Lee BR, You S, Kim EJ, Kim JN, Song E, Yang YH, Hwang D, Kim BG. Appl. Microbiol. Biotechnol. 102 3243-3253 (2018)


Quick links