Biology:Ferric uptake regulator family

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FUR
PDB 1mzb EBI.jpg
ferric uptake regulator
Identifiers
SymbolFUR
PfamPF01475
Pfam clanCL0123
InterProIPR002481
SCOP21mzb / SCOPe / SUPFAM
Ferric uptake regulatory protein
Identifiers
OrganismEscherichia coli
SymbolFur
PDB2FU4 (ECOD)
UniProtP0A9A9

In molecular biology, the ferric uptake regulator family is a family of bacterial proteins involved in regulating metal ion uptake and in metal homeostasis. The family is named for its founding member, known as the ferric uptake regulator or ferric uptake regulatory protein (Fur). Fur proteins are responsible for controlling the intracellular concentration of iron in many bacteria. Iron is essential for most organisms, but its concentration must be carefully managed over a wide range of environmental conditions; high concentrations can be toxic due to the formation of reactive oxygen species.[1]

Function

Members of the ferric uptake regulator family are transcription factors that primarily exert their regulatory effects as repressors: when bound to their cognate metal ion, they are capable of binding DNA and preventing expression of the genes they regulate, but under low concentrations of metal, they undergo a conformational change that prevents DNA binding and lifts the repression.[2][3] In the case of the ferric uptake regulator protein itself, its immediate downstream target is a noncoding RNA called RyhB.[2]

In addition to the ferric uptake regulator protein, members of the Fur family are also involved in maintaining homeostasis with respect to other ions:[4]

The iron dependent repressor family is a functionally similar but non-homologous family of proteins involved in iron homeostasis in prokaryotes.[1]

Relationship to virulence

Metal homeostasis can be a factor in bacterial virulence, an observation with a particularly long history in the case of iron.[15][16][17] In some cases, expression of virulence factors is under the regulatory control of the Fur protein.[1][2]

References

  1. ↑ 1.0 1.1 1.2 "Architecture of a protein central to iron homeostasis: crystal structure and spectroscopic analysis of the ferric uptake regulator". Molecular Microbiology 47 (4): 903–15. February 2003. doi:10.1046/j.1365-2958.2003.03337.x. PMID 12581348. 
  2. ↑ 2.0 2.1 2.2 "Interplay between iron homeostasis and virulence: Fur and RyhB as major regulators of bacterial pathogenicity". Veterinary Microbiology 179 (1–2): 2–14. August 2015. doi:10.1016/j.vetmic.2015.03.024. PMID 25888312. https://zenodo.org/record/997453. 
  3. ↑ "Structural and mechanistic basis of zinc regulation across the E. coli Zur regulon". PLOS Biology 12 (11): e1001987. November 2014. doi:10.1371/journal.pbio.1001987. PMID 25369000. 
  4. ↑ "How do bacterial cells ensure that metalloproteins get the correct metal?". Nature Reviews. Microbiology 7 (1): 25–35. January 2009. doi:10.1038/nrmicro2057. PMID 19079350. 
  5. ↑ "The Fur-like protein Mur of Rhizobium leguminosarum is a Mn(2+)-responsive transcriptional regulator". Microbiology 150 (Pt 5): 1447–56. May 2004. doi:10.1099/mic.0.26961-0. PMID 15133106. 
  6. ↑ "Fur is involved in manganese-dependent regulation of mntA (sitA) expression in Sinorhizobium meliloti". Applied and Environmental Microbiology 70 (7): 4349–55. July 2004. doi:10.1128/AEM.70.7.4349-4355.2004. PMID 15240318. Bibcode: 2004ApEnM..70.4349P. 
  7. ↑ "The Sinorhizobium meliloti fur gene regulates, with dependence on Mn(II), transcription of the sitABCD operon, encoding a metal-type transporter". Journal of Bacteriology 186 (11): 3609–20. June 2004. doi:10.1128/JB.186.11.3609-3620.2004. PMID 15150249. 
  8. ↑ "The mntH gene encodes the major Mn(2+) transporter in Bradyrhizobium japonicum and is regulated by manganese via the Fur protein". Molecular Microbiology 72 (2): 399–409. April 2009. doi:10.1111/j.1365-2958.2009.06650.x. PMID 19298371. 
  9. ↑ "Mur regulates the gene encoding the manganese transporter MntH in Brucella abortus 2308". Journal of Bacteriology 194 (3): 561–6. February 2012. doi:10.1128/JB.05296-11. PMID 22101848. 
  10. ↑ "Nur, a nickel-responsive regulator of the Fur family, regulates superoxide dismutases and nickel transport in Streptomyces coelicolor". Molecular Microbiology 59 (6): 1848–58. March 2006. doi:10.1111/j.1365-2958.2006.05065.x. PMID 16553888. 
  11. ↑ "The PerR transcription factor senses H2O2 by metal-catalysed histidine oxidation". Nature 440 (7082): 363–7. March 2006. doi:10.1038/nature04537. PMID 16541078. Bibcode: 2006Natur.440..363L. 
  12. ↑ "Severe zinc depletion of Escherichia coli: roles for high affinity zinc binding by ZinT, zinc transport and zinc-independent proteins". The Journal of Biological Chemistry 284 (27): 18377–89. July 2009. doi:10.1074/jbc.M109.001503. PMID 19377097. 
  13. ↑ "Advances in the molecular understanding of biological zinc transport". Chemical Communications 51 (22): 4544–63. March 2015. doi:10.1039/c4cc10174j. PMID 25627157. http://wrap.warwick.ac.uk/76059/1/WRAP_Blindauer_C4CC10174J.pdf. 
  14. ↑ "Perception and Homeostatic Control of Iron in the Rhizobia and Related Bacteria". Annual Review of Microbiology 69: 229–45. 2015. doi:10.1146/annurev-micro-091014-104432. PMID 26195304. 
  15. ↑ "Role of Iron in Bacterial Infection". Modern Aspects of Electrochemistry. 80. 1978. 1–35. doi:10.1007/978-3-642-66956-9_1. ISBN 978-1-4612-9003-2. 
  16. ↑ "Iron metabolism in pathogenic bacteria". Annual Review of Microbiology 54: 881–941. 2000. doi:10.1146/annurev.micro.54.1.881. PMID 11018148. 
  17. ↑ "Role of iron in regulation of virulence genes". Clinical Microbiology Reviews 6 (2): 137–49. April 1993. doi:10.1128/cmr.6.2.137. PMID 8472246. 
This article incorporates text from the public domain Pfam and InterPro: IPR002481



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