This Article
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 Troup, B.
Right arrow Articles by Jahn, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Troup, B.
Right arrow Articles by Jahn, D.

 Previous Article  |  Next Article 

J. Bacteriol., Jun 1995, 3326-3331, Vol 177, No. 11
Copyright © 1995, American Society for Microbiology

Cloning and characterization of the Escherichia coli hemN gene encoding the oxygen-independent coproporphyrinogen III oxidase

B Troup, C Hungerer and D Jahn
Laboratorium fur Mikrobiologie, Fachbereich Biologie, Philipps- Universitat Marburg, Germany.

Coproporphyrinogen III oxidase, an enzyme involved in heme biosynthesis, catalyzes the oxidative decarboxylation of coproporphyrinogen III to form protoporphyrinogen IX. Genetic and biochemical studies suggested the presence of two different coproporphyrinogen III oxidases, one for aerobic (HemF) and one for anaerobic (HemN) conditions. Here we report the cloning of the hemN gene encoding the oxygen-independent coproporphyrinogen III oxidase from Escherichia coli by complementation of a Salmonella typhimurium hemF hemN double mutant. An open reading frame of 1,371 bp encoding a protein of 457 amino acids with a calculated molecular mass of 52.8 kDa was identified. Sequence comparisons revealed 92% amino acid sequence identity to the recently cloned S. typhimurium hemN gene and 35% identity to the Rhodobacter sphaeroides gene. The hemN gene was mapped to 87.3 min of the E. coli chromosome and found identical to open reading frame o459 previously discovered during the genome sequencing project. Complementation of S. typhimurium hemF hemN double mutants with the E. coli hemN gene was detected under aerobic and anaerobic conditions, indicating an aerobic function for HemN. The previously cloned E. coli hemF gene encoding the oxygen-dependent enzyme complemented exclusively under aerobic conditions. Primer extension experiments revealed a strong transcription initiation site 102 bp upstream of the translational start site. DNA sequences with homology to a sigma 70-dependent promoter were detected. Expression of the hemN gene in response to changing environmental conditions was evaluated by using lacZ reporter gene fusions. Under anaerobic conditions, hemN expression was threefold greater than under aerobic growth conditions.(ABSTRACT TRUNCATED AT 250 WORDS)


This article has been cited by other articles:

  • Tatsumi, R., Wachi, M. (2008). TolC-Dependent Exclusion of Porphyrins in Escherichia coli. J. Bacteriol. 190: 6228-6233 [Abstract] [Full Text]  
  • Ouchane, S., Picaud, M., Therizols, P., Reiss-Husson, F., Astier, C. (2007). Global Regulation of Photosynthesis and Respiration by FnrL: THE FIRST TWO TARGETS IN THE TETRAPYRROLE PATHWAY. J. Biol. Chem. 282: 7690-7699 [Abstract] [Full Text]  
  • Zeilstra-Ryalls, J. H., Schornberg, K. L. (2006). Analysis of hemF Gene Function and Expression in Rhodobacter sphaeroides 2.4.1. J. Bacteriol. 188: 801-804 [Abstract] [Full Text]  
  • Wyckoff, E. E., Schmitt, M., Wilks, A., Payne, S. M. (2004). HutZ Is Required for Efficient Heme Utilization in Vibrio cholerae. J. Bacteriol. 186: 4142-4151 [Abstract] [Full Text]  
  • Breckau, D., Mahlitz, E., Sauerwald, A., Layer, G., Jahn, D. (2003). Oxygen-dependent Coproporphyrinogen III Oxidase (HemF) from Escherichia coli Is Stimulated by Manganese. J. Biol. Chem. 278: 46625-46631 [Abstract] [Full Text]  
  • Layer, G., Verfurth, K., Mahlitz, E., Jahn, D. (2002). Oxygen-independent Coproporphyrinogen-III Oxidase HemN from Escherichia coli. J. Biol. Chem. 277: 34136-34142 [Abstract] [Full Text]  
  • Fischer, H.-M., Velasco, L., Delgado, M. J., Bedmar, E. J., Schären, S., Zingg, D., Göttfert, M., Hennecke, H. (2001). One of Two hemN Genes in Bradyrhizobium japonicum Is Functional during Anaerobic Growth and in Symbiosis. J. Bacteriol. 183: 1300-1311 [Abstract] [Full Text]  
  • Holtzendorff, J., Partensky, F., Jacquet, S., Bruyant, F., Marie, D., Garczarek, L., Mary, I., Vaulot, D., Hess, W. R. (2001). Diel Expression of Cell Cycle-Related Genes in Synchronized Cultures of Prochlorococcus sp. Strain PCC 9511. J. Bacteriol. 183: 915-920 [Abstract] [Full Text]  
  • Homuth, G., Rompf, A., Schumann, W., Jahn, D. (1999). Transcriptional Control of Bacillus subtilis hemN and hemZ. J. Bacteriol. 181: 5922-5929 [Abstract] [Full Text]  
  • Yeliseev, A. A., Kaplan, S. (1999). A Novel Mechanism for the Regulation of Photosynthesis Gene Expression by the TspO Outer Membrane Protein of Rhodobacter sphaeroides 2.4.1. J. Biol. Chem. 274: 21234-21243 [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»