The cbb3 oxidases are an ancient innovation of the domain bacteria

A survey of genomes for the presence of gene clusters related to cbb(3) oxidases detected bona fide members of the family in almost all phyla of the domain Bacteria. No archaeal representatives were found. The subunit composition was seen to vary substantially between clades observed on the phylogen...

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Published inMolecular biology and evolution Vol. 25; no. 6; pp. 1158 - 1166
Main Authors Ducluzeau, Anne-Lise, Ouchane, Soufian, Nitschke, Wolfgang
Format Journal Article
LanguageEnglish
Published United States 01.06.2008
Subjects
Bacterial Proteins - classification
Bacterial Proteins - genetics
Catalytic Domain - genetics
Electron Transport Complex IV - classification
Electron Transport Complex IV - genetics
Evolution, Molecular
Genome, Bacterial
Hemeproteins - classification
Hemeproteins - genetics
Multigene Family
Phylogeny
Protein Subunits - classification
Protein Subunits - genetics
Sequence Analysis, DNA
Online AccessGet full text

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Abstract A survey of genomes for the presence of gene clusters related to cbb(3) oxidases detected bona fide members of the family in almost all phyla of the domain Bacteria. No archaeal representatives were found. The subunit composition was seen to vary substantially between clades observed on the phylogenetic tree of the catalytic subunit CcoN. The protein diade formed by CcoN and the monoheme cytochrome CcoO appears to constitute the functionally essential "core" of the enzyme conserved in all sampled cbb(3) gene clusters. The topology of the phylogenetic tree contradicts the scenario of a recent origin of cbb(3) oxidases and substantiates the status of this family as a phylogenetic entity on the same level as the other subgroups of the heme-copper superfamily (including nitric oxide reductase). This finding resuscitates and exacerbates the conundrum of the evolutionary origin of heme-copper oxidases.
AbstractList A survey of genomes for the presence of gene clusters related to cbb(3) oxidases detected bona fide members of the family in almost all phyla of the domain Bacteria. No archaeal representatives were found. The subunit composition was seen to vary substantially between clades observed on the phylogenetic tree of the catalytic subunit CcoN. The protein diade formed by CcoN and the monoheme cytochrome CcoO appears to constitute the functionally essential "core" of the enzyme conserved in all sampled cbb(3) gene clusters. The topology of the phylogenetic tree contradicts the scenario of a recent origin of cbb(3) oxidases and substantiates the status of this family as a phylogenetic entity on the same level as the other subgroups of the heme-copper superfamily (including nitric oxide reductase). This finding resuscitates and exacerbates the conundrum of the evolutionary origin of heme-copper oxidases.
Author Nitschke, Wolfgang
Ouchane, Soufian
Ducluzeau, Anne-Lise
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  surname: Nitschke
  fullname: Nitschke, Wolfgang
BackLink https://www.ncbi.nlm.nih.gov/pubmed/18353797$$D View this record in MEDLINE/PubMed
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Snippet A survey of genomes for the presence of gene clusters related to cbb(3) oxidases detected bona fide members of the family in almost all phyla of the domain...
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StartPage 1158
SubjectTerms Bacterial Proteins - classification
Bacterial Proteins - genetics
Catalytic Domain - genetics
Electron Transport Complex IV - classification
Electron Transport Complex IV - genetics
Evolution, Molecular
Genome, Bacterial
Hemeproteins - classification
Hemeproteins - genetics
Multigene Family
Phylogeny
Protein Subunits - classification
Protein Subunits - genetics
Sequence Analysis, DNA
Title The cbb3 oxidases are an ancient innovation of the domain bacteria
URI https://www.ncbi.nlm.nih.gov/pubmed/18353797
https://search.proquest.com/docview/69208311
Volume 25
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