7
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Prokaryotic origins for the mitochondrial alternative oxidase and plastid terminal oxidase nuclear genes.

        1 , ,
      FEBS letters

      Read this article at

      ScienceOpenPublisherPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          The mitochondrial alternative oxidase is a diiron carboxylate quinol oxidase (Dox) found in plants and some fungi and protists, but not animals. The plastid terminal oxidase is distantly related to alternative oxidase and is most likely also a Dox protein. Database searches revealed that the alpha-proteobacterium Novosphingobium aromaticivorans and the cyanobacteria Nostoc sp. PCC7120, Synechococcus sp. WH8102 and Prochlorococcus marinus subsp. pastoris CCMP1378 each possess a Dox homolog. Each prokaryotic protein conforms to the current structural models of the Dox active site and phylogenetic analyses suggest that the eukaryotic Dox genes arose from an ancestral prokaryotic gene.

          Related collections

          Author and article information

          Journal
          FEBS Lett.
          FEBS letters
          0014-5793
          0014-5793
          Dec 18 2003
          : 555
          : 3
          Affiliations
          [1 ] Plant Molecular Biology Group and School of Plant Biology, University of Western Australia, 35 Stirling Highway, Crawley, WA 6009, Australia. pfinnega@agric.uwa.edu.au
          Article
          S0014579303013097
          10.1016/S0014-5793(03)01309-7
          14675750
          65e09855-a1a3-4df8-af08-5061bf4d9dca
          History

          Comments

          Comment on this article