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Related Experiment Videos

Characterization of Bacillus subtilis hemN

B Hippler1, G Homuth, T Hoffmann

  • 1Abteilung Biochemie, Max-Planck-Institut für Terrestrische Mikrobiologie, Marburg, Germany.

Journal of Bacteriology
|November 26, 1997
PubMed
Summary

Bacillus subtilis hemN facilitates oxygen-independent coproporphyrinogen III decarboxylation. Despite normal growth, a hemN mutant accumulates this compound anaerobically, suggesting a second hemN-like gene in B. subtilis.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • The biosynthesis of heme, a vital prosthetic group, involves multiple enzymatic steps.
  • Coproporphyrinogen III decarboxylation is a key step in heme biosynthesis.
  • The specific genes and pathways involved in B. subtilis heme biosynthesis, particularly under anaerobic conditions, require further elucidation.

Purpose of the Study:

  • To characterize the function of the Bacillus subtilis hemN gene, identified upstream of the dnaK operon.
  • To investigate the role of hemN in coproporphyrinogen III decarboxylation under aerobic and anaerobic conditions.
  • To explore the genetic organization and regulation of the hemN gene in B. subtilis.

Main Methods:

  • Functional complementation assays using Salmonella typhimurium hemF hemN double mutants.

Related Experiment Videos

  • Growth experiments with a B. subtilis hemN mutant under aerobic and anaerobic conditions.
  • Northern blot analysis to determine hemN transcript levels and organization.

    • Main Results:

    • B. subtilis hemN successfully complemented S. typhimurium hemF hemN mutants, indicating its role in coproporphyrinogen III decarboxylation.
    • A B. subtilis hemN mutant accumulated coproporphyrinogen III exclusively under anaerobic growth.
    • The hemN gene is part of a pentacistronic transcript (lepA, hemN, hrcA, grpE, dnaK) with similar expression under aerobic and anaerobic conditions.
    • No evidence for hemF in B. subtilis was found, and B. subtilis hemY could not rescue the S. typhimurium hemF hemN deficiency.

    Conclusions:

    • B. subtilis hemN encodes a protein essential for oxygen-independent coproporphyrinogen III decarboxylation.
    • The presence of an alternative oxygen-independent pathway for this reaction is suggested by the normal growth of the hemN mutant.
    • The results strongly indicate the absence of a hemF homolog in B. subtilis and suggest the existence of a second hemN-like gene.