MISC

2002年2月

Diversity of ammonia monooxygenase operon in autotrophic ammonia-oxidizing bacteria

ARCHIVES OF MICROBIOLOGY
  • JM Norton
  • ,
  • JJ Alzerreca
  • ,
  • Y Suwa
  • ,
  • MG Klotz

177
2
開始ページ
139
終了ページ
149
記述言語
英語
掲載種別
DOI
10.1007/s00203-001-0369-z
出版者・発行元
SPRINGER-VERLAG

Autotrophic ammonia-oxidizing bacteria use the essential enzyme ammonia monooxygenase (AMO) to transform ammonia to hydroxylamine. The amo operon consists of at least three genes, amoC, amoA, and amoB; amoA encodes the subunit containing the putative enzyme active site. The use of the auto genes as functional markers for ammonia-oxidizing bacteria in environmental applications requires knowledge of the diversity of the amo operon on several levels: (1) the copy number of the operon in the genome, (2) the arrangement of the three genes in an individual operon, and (3) the primary sequence of the individual genes. We present a database of amo gene sequences for pure cultures of ammonia-oxidizing bacteria representing both the beta- and the gamma-subdivision of Proteobacteria in the following genera: Nitrosospira (6 strains), Nitrosomonas (5 strains) and Nitrosococcus (2 strains). The amo operon was found in multiple (2-3) nearly identical copies in the beta-subdivision representatives but in single copies in the gamma-subdivision ammonia oxidizers. The analysis of the deduced amino acid sequence revealed strong conservation for all three Amo peptides in both primary and secondary structures. For the amoA gene within the gamma-subdivision, nucleotide identity values are approximately 85% within the Nitrosomonas or the Nitrosospira groups, but approximately 75% when comparing between these groups. Conserved regions in amoA and amoC were identified and used as primer sites for PCR amplification of amo genes from pure cultures, enrichments and the soil environment. The intergenic region between amoC and amoA is variable in length and may be used to profile the community of ammonia-oxidizing bacteria in environmental samples. Electronic supplementary material to this paper can be obtained by using the Springer LINK server located at http://dx.doi.org/10.1007/s00203-001-0369-z..

リンク情報
DOI
https://doi.org/10.1007/s00203-001-0369-z
CiNii Articles
http://ci.nii.ac.jp/naid/80012892456
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/11807563
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000174205400003&DestApp=WOS_CPL
ID情報
  • DOI : 10.1007/s00203-001-0369-z
  • ISSN : 0302-8933
  • CiNii Articles ID : 80012892456
  • identifiers.cinii_nr_id : 9000239248799
  • PubMed ID : 11807563
  • Web of Science ID : WOS:000174205400003

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