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Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases.
Department of Biology, University of California at San Diego, La Jolla 92093-0116, USA.
Thirty-eight ATP-binding cassette (ABC) protein constituents of bacterial extracytoplasmic receptor-dependent nutrient uptake systems, including one homologous chloroplast protein were analysed for sequence conservation and phylogenetic relatedness. The proteins were generally found to cluster in accordance with the clustering patterns previously observed for the extracytoplasmic receptors and the transmembrane channel-forming constituents of these permeases. The results suggest that these transport systems evolved from a single primordial system with minimal shuffling of the three dissimilar protein constituents of the systems.
PMID: 7569321 [PubMed - indexed for MEDLINE]
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Cited by 5 PubMed Central articles
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ReviewStructure, function, and evolution of bacterial ATP-binding cassette systems.
Davidson AL, Dassa E, Orelle C, Chen J.
Microbiol Mol Biol Rev. 2008 Jun; 72(2):317-64, table of contents.
[Microbiol Mol Biol Rev. 2008]
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Evolutionary primacy of sodium bioenergetics.
Mulkidjanian AY, Galperin MY, Makarova KS, Wolf YI, Koonin EV.
Biol Direct. 2008 Apr 1; 3:13. Epub 2008 Apr 1.
[Biol Direct. 2008]
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A phylogenomic analysis of the Actinomycetales mce operons.
Casali N, Riley LW.
BMC Genomics. 2007 Feb 26; 8:60. Epub 2007 Feb 26.
[BMC Genomics. 2007]
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