Evidence that participate methane monooxygenase and ammonia monooxygenase may be evolutionarily related

Andrew J. Holmes, Andria Costello, Mary E. Lidstrom, J. Colin Murrell

Research output: Contribution to journalArticle

613 Scopus citations

Abstract

Genes encoding paniculate methane monooxygenase and ammonia monooxygenase share high sequence identity. Degenerate oligonucleotide primers were designed, based on regions of shared amino acid sequence between the 27-kDa polypeptides, which are believed to contain the active sites, of particulate methane monooxygenase and ammonia monooxygenase. A 525-bp internal DNA fragment of the genes encoding these polypeptides (pmoA and amoA) from a variety of methanotrophic and nitrifying bacteria was amplified by PCR, cloned and sequenced. Representatives of each of the phylogenetic groups of both methanotrophs ( α- and γ-Proteobacteria) and ammonia-oxidizing nitrifying bacteria ( β-and y-Proteobacteria) were included. Analysis of the predicted amino acid sequences of these genes revealed strong conservation of both primary and secondary structure. Nitrosococcus oceanus AmoA showed higher identity to PmoA sequences from other members of the γ-Proteobacteria than to AmoA sequences. These results suggest that the particulate methane monooxygenase and ammonia monooxygenase are evolutionarily related enzymes despite their different physiological roles in these bacteria.

Original languageEnglish (US)
Pages (from-to)203-208
Number of pages6
JournalFEMS Microbiology Letters
Volume132
Issue number3
DOIs
StatePublished - Oct 15 1995
Externally publishedYes

Keywords

  • Ammonia monooxygenase
  • Methane monooxygenase
  • Methanotroph
  • Nitrifier

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Genetics

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