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Related Experiment Videos

Urease-encoding genes in ammonia-oxidizing bacteria.

Teresa E Koper1, Amal F El-Sheikh, Jeanette M Norton

  • 1Departments of Biology, Utah State University, Logan, Utah 84322-4820, USA.

Applied and Environmental Microbiology
|April 7, 2004
PubMed
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Ammonia-oxidizing bacteria (AOB) possess urease genes, crucial for urea metabolism. This study sequenced urease operons in AOB, revealing conserved gene structures and evolutionary insights into urease in Proteobacteria.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Evolutionary Biology

Background:

  • Many ammonia-oxidizing bacteria (AOB) produce urease (urea amidohydrolase), enabling urea utilization for chemolithotrophic growth.
  • Urease activity is significant in the nitrogen cycle and microbial ecology, yet its genetic basis in diverse AOB remains incompletely understood.

Purpose of the Study:

  • To sequence and characterize urease operons in beta- and gamma-proteobacterial AOB.
  • To develop molecular tools for identifying ureolytic AOB ecotypes.
  • To investigate the evolutionary history of urease genes in AOB.

Main Methods:

  • Sequencing of urease operons (ureABC, ureD, ureEFG) from Nitrosospira sp. strain NpAV and Nitrosococcus oceani.
  • Green fluorescent protein reporter gene fusions to analyze gene expression.

Related Experiment Videos

  • Southern analyses to determine gene copy numbers.
  • Phylogenetic analysis of ureC gene sequences from various AOB and public databases.

    • Main Results:

    • The complete urease operon structure (ureD-ureABC-ureEFG) was identified in both studied AOB.
    • Nitrosospira sp. strain NpAV possesses two copies of ureC, while Nitrosococcus oceani has one.
    • Phylogenetic analysis revealed that beta-proteobacterial AOB ureC genes form a distinct group, unexpectedly diverging from other beta-proteobacteria.
    • Conserved and variable sequence motifs within ureC were identified for potential use in environmental AOB detection.

    Conclusions:

    • The conserved structure of the urease operon in AOB suggests a common evolutionary origin.
    • The phylogenetic placement of AOB urease suggests ancient divergence predating the speciation of major proteobacterial groups.
    • Identified conserved and variable regions in ureC provide a foundation for developing molecular probes for environmental AOB research.