The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
A suf operon requirement for Fe–S cluster assembly during iron starvation in Escherichia coli
Open accessAbstract
Summary: The suf and isc operons of Escherichia coli have been implicated in Fe–S cluster assembly. However, it has been unclear why E. coli has two systems for Fe–S cluster biosynthesis. We have examined the regulatory characteristics and mutant phenotypes of both operons to discern if the two operons have redundant functions or if their cellular roles are divergent. Both operons are similarly induced by hydrogen peroxide and the iron chelator 2,2′‐dipyridyl, although by different mechanisms. Regulation of the isc operon is mediated by IscR, whereas the suf operon requires OxyR and IHF for the response to oxidative stress and Fur for induction by iron starvation. Simultaneous deletion of iscS and most suf genes is synthetically lethal. However, although the suf and isc operons have overlapping functions, they act as distinct complexes because the SufS desulphurase alone cannot substitute for the IscS enzyme. In addition, suf deletion mutants are more sensitive to iron starvation than isc mutants, and the activity of the Fe–S enzyme gluconate dehydratase is diminished in the suf mutant during iron starvation. These findings are consistent with the model that the isc operon encodes the housekeeping Fe–S cluster assembly system in E. coli, whereas the suf operon is specifically adapted to synthesize Fe–S clusters when iron or sulphur metabolism is disrupted by iron starvation or oxidative stress.
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Cites
One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
Datsenko, K. A., & Wanner, B. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.120163297 · Cited by 14,782
An efficient recombination system for chromosome engineering in Escherichia coli
Yu, D., Ellis, H. M., Lee, E.-C., Jenkins, N. A., Copeland, N. G., & Court, D. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.100127597 · Cited by 1,688
Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro
Imlay, J. A., Chin, S. M., & Linn, S. (1988) · Science · doi:10.1126/science.2834821 · Cited by 1,555 · cited 2×
“Restricting iron uptake and sequestering intracellular iron during H2O2 stress protects the cell from the Fenton reaction whereby Fe2+ reacts with H2O2 to form hydroxyl radicals (Imlay et al., 1988).”
BackgroundZheng, M., Wang, X., Templeton, L. J., Smulski, D. R., LaRossa, R. A., & Storz, G. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.15.4562-4570.2001 · Cited by 808
Self-citationAssembly of Iron-Sulfur Clusters
Zheng, L., Cash, V. L., Flint, D. H., & Dean, D. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.13264 · Cited by 649
Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis.
Zheng, L., White, R. H., Cash, V. L., Jack, R. F., & Dean, D. R. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.7.2754 · Cited by 595
Global Iron-dependent Gene Regulation in Escherichia coli
McHugh, J. P., Rodríguez-Quiñones, F., Abdul-Tehrani, H., Svistunenko, D. A., Poole, R. K., Cooper, C. E., & Andrews, S. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303381200 · Cited by 468
Takahashi, Y., & Tokumoto, U. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200365200 · Cited by 456
Schwartz, C. J., Giel, J. L., Patschkowski, T., Luther, C., Ruzicka, F. J., Beinert, H., & Kiley, P. J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251550898 · Cited by 443
The dps promoter is activated by OxyR during growth and by IHF and σs in stationary phase
Altuvia, S., Almiron, M., Huisman, G., Kolter, R., & Storz, G. (1994) · Molecular Microbiology · doi:10.1111/j.1365-2958.1994.tb00421.x · Cited by 437
Self-citation
Cited by
Cellular Defenses against Superoxide and Hydrogen Peroxide
Imlay, J. A. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.061606.161055 · Cited by 1,563
Structure, function, and formation of biological iron-sulfur clusters
Johnson, D. C., Dean, D. R., Smith, A. D., & Johnson, M. K. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133518 · Cited by 1,438
Song, H., Yoo, Y., Hwang, J., Na, Y.-C., & Kim, H. S. (2016) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2015.08.021 · Cited by 416
eSGA: E. coli synthetic genetic array analysis
Butland, G., Babu, M., Díaz-Mejía, J. J., Bohdana, F., Phanse, S., Gold, B., Yang, W., Li, J., Gagarinova, A. G., Pogoutse, O., et al. (2008) · Nature Methods · doi:10.1038/nmeth.1239 · Cited by 256
Peroxide Stress Elicits Adaptive Changes in Bacterial Metal Ion Homeostasis
Faulkner, M. J., & Helmann, J. D. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3682 · Cited by 151
Metadata
- Authors
- Outten, F. W., Djaman, O., & Storz, G.
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2004-04
- Volume
- 52
- Issue
- 3
- Pages
- 861-872
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- OpenAlex
- W2157433322
- Cited by
- 448
- References
- 48
- FWCI
- 18.78
- Type
- journal article
- Language
- en
- Open access
- bronze
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