This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Skovran, E.
Right arrow Articles by Downs, D. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Skovran, E.
Right arrow Articles by Downs, D. M.

 Previous Article  |  Next Article 

Journal of Bacteriology, January 2003, p. 98-106, Vol. 185, No. 1
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.1.98-106.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Lack of the ApbC or ApbE Protein Results in a Defect in Fe-S Cluster Metabolism in Salmonella enterica Serovar Typhimurium

Elizabeth Skovran and Diana M. Downs*

Department of Bacteriology, University of Wisconsin-Madison, Madison, Wisconsin 53706

Received 11 September 2002/ Accepted 6 October 2002

The isc genes function in the assembly of Fe-S clusters and are conserved in many prokaryotic and eukaryotic organisms. In most bacteria studied, the isc operon can be deleted without loss of cell viability, indicating that additional systems for Fe-S cluster assembly must exist. Several laboratories have described nutritional and biochemical defects resulting from mutations in the isc operon. Here we demonstrate that null mutations in two genes of unknown function, apbC and apbE, result in similar cellular deficiencies. Exogenous ferric chloride suppressed these deficiencies in the apbC and apbE mutants, distinguishing them from previously described isc mutants. The deficiencies caused by the apbC and isc mutations were additive, which is consistent with Isc and ApbC's having redundant functions or with Isc and ApbC's functioning in different areas of Fe-S cluster metabolism (e.g., Fe-S cluster assembly and Fe-S cluster repair). Both the ApbC and ApbE proteins are similar in sequence to proteins that function in metal cofactor assembly. Like the enzymes with sequence similarity to ApbC, purified ApbC protein was able to hydrolyze ATP. The data herein are consistent with the hypothesis that the ApbC and ApbE proteins function in Fe-S cluster metabolism in vivo.

* Corresponding author. Mailing address: University of Wisconsin-Madison, 1550 Linden Dr., Madison, WI 53706. Phone: (608) 265-4630. Fax: (608) 262-9865. E-mail: downs{at}bact.wisc.edu.

Journal of Bacteriology, January 2003, p. 98-106, Vol. 185, No. 1
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.1.98-106.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Lewis, J. A., Boyd, J. M., Downs, D. M., Escalante-Semerena, J. C. (2009). Involvement of the Cra Global Regulatory Protein in the Expression of the iscRSUA Operon, Revealed during Studies of Tricarballylate Catabolism in Salmonella enterica. J. Bacteriol. 191: 2069-2076 [Abstract] [Full Text]  
  • Boyd, J. M., Drevland, R. M., Downs, D. M., Graham, D. E. (2009). Archaeal ApbC/Nbp35 Homologs Function as Iron-Sulfur Cluster Carrier Proteins. J. Bacteriol. 191: 1490-1497 [Abstract] [Full Text]  
  • Boyd, J. M., Sondelski, J. L., Downs, D. M. (2009). Bacterial ApbC Protein Has Two Biochemical Activities That Are Required for in Vivo Function. J. Biol. Chem. 284: 110-118 [Abstract] [Full Text]  
  • Thorgersen, M. P., Downs, D. M. (2009). Oxidative stress and disruption of labile iron generate specific auxotrophic requirements in Salmonella enterica. Microbiology 155: 295-304 [Abstract] [Full Text]  
  • Stehling, O., Netz, D. J. A., Niggemeyer, B., Rosser, R., Eisenstein, R. S., Puccio, H., Pierik, A. J., Lill, R. (2008). Human Nbp35 Is Essential for both Cytosolic Iron-Sulfur Protein Assembly and Iron Homeostasis. Mol. Cell. Biol. 28: 5517-5528 [Abstract] [Full Text]  
  • Boyd, J. M., Lewis, J. A., Escalante-Semerena, J. C., Downs, D. M. (2008). Salmonella enterica Requires ApbC Function for Growth on Tricarballylate: Evidence of Functional Redundancy between ApbC and IscU. J. Bacteriol. 190: 4596-4602 [Abstract] [Full Text]  
  • Ayala-Castro, C., Saini, A., Outten, F. W. (2008). Fe-S Cluster Assembly Pathways in Bacteria. Microbiol. Mol. Biol. Rev. 72: 110-125 [Abstract] [Full Text]  
  • Thorgersen, M. P., Downs, D. M. (2007). Cobalt Targets Multiple Metabolic Processes in Salmonella enterica. J. Bacteriol. 189: 7774-7781 [Abstract] [Full Text]  
  • Dougherty, M. J., Downs, D. M. (2006). A connection between iron-sulfur cluster metabolism and the biosynthesis of 4-amino-5-hydroxymethyl-2-methylpyrimidine pyrophosphate in Salmonella enterica.. Microbiology 152: 2345-2353 [Abstract] [Full Text]  
  • Vivas, E., Skovran, E., Downs, D. M. (2006). Salmonella enterica Strains Lacking the Frataxin Homolog CyaY Show Defects in Fe-S Cluster Metabolism In Vivo. J. Bacteriol. 188: 1175-1179 [Abstract] [Full Text]  
  • Masse, E., Vanderpool, C. K., Gottesman, S. (2005). Effect of RyhB Small RNA on Global Iron Use in Escherichia coli. J. Bacteriol. 187: 6962-6971 [Abstract] [Full Text]  
  • Hausmann, A., Aguilar Netz, D. J., Balk, J., Pierik, A. J., Muhlenhoff, U., Lill, R. (2005). The eukaryotic P loop NTPase Nbp35: An essential component of the cytosolic and nuclear iron-sulfur protein assembly machinery. Proc. Natl. Acad. Sci. USA 102: 3266-3271 [Abstract] [Full Text]  
  • Loo, C. Y., Mitrakul, K., Jaafar, S., Gyurko, C., Hughes, C. V., Ganeshkumar, N. (2004). Role of a nosX Homolog in Streptococcus gordonii in Aerobic Growth and Biofilm Formation. J. Bacteriol. 186: 8193-8206 [Abstract] [Full Text]  
  • Skovran, E., Lauhon, C. T., Downs, D. M. (2004). Lack of YggX Results in Chronic Oxidative Stress and Uncovers Subtle Defects in Fe-S Cluster Metabolism in Salmonella enterica. J. Bacteriol. 186: 7626-7634 [Abstract] [Full Text]  
  • Martinez-Gomez, N. C., Robers, M., Downs, D. M. (2004). Mutational Analysis of ThiH, a Member of the Radical S-Adenosylmethionine (AdoMet) Protein Superfamily. J. Biol. Chem. 279: 40505-40510 [Abstract] [Full Text]  
  • Leonardi, R., Roach, P. L. (2004). Thiamine Biosynthesis in Escherichia coli: IN VITRO RECONSTITUTION OF THE THIAZOLE SYNTHASE ACTIVITY. J. Biol. Chem. 279: 17054-17062 [Abstract] [Full Text]  
  • Gralnick, J. A., Downs, D. M. (2003). The YggX Protein of Salmonella enterica Is Involved in Fe(II) Trafficking and Minimizes the DNA Damage Caused by Hydroxyl Radicals: RESIDUE CYS-7 IS ESSENTIAL FOR YggX FUNCTION. J. Biol. Chem. 278: 20708-20715 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»