Journal of Molecular Evolution

, Volume 29, Issue 2, pp 157–169

Evolutionary conservation of protein regions in the protonmotive cytochromeb and their possible roles in redox catalysis

  • Neil Howell
Article

Summary

The amino acid sequences of the protonmotive cytochromeb from seven representative and phylogenetically diverse species have been compared to identify protein regions or segments that are conserved during evolution. The sequences analyzed included both prokaryotic and eukaryotic examples as well as mitochondrial cytochromeb and chloroplastb6 proteins. The principal conclusion from these analyses is that there are five protein regions-each comprising about 20 amino acid residues—that are consistently conserved during evolution. These domains are evident despite the low density of invariant residues. The two most highly conserved regions, spanning approximately consensus residues 130–150 and 270–290, are located in extramembrane loops and are hypothesized to constitute part of the Qo reaction center. The intramembrane, hydrophobic protein regions containing the heme-ligating histidines are also conserved during evolution. It was found, however, that the conservation of the protein segments extramembrane to the histidine residues ligating the low potential b566 heme group showed a higher degree of sequence conservation. The location of these conserved regions suggests that these extramembrane segments are also involved in forming the Qo reaction center. A protein segment putatively constituting a portion of the Qi reaction center, located approximately in the region spanned by consensus residues 20–40, is conserved in species as divergent as mouse andRhodobacter. This region of the protein shows substantially less sequence conservation in the chloroplast cytochromeb6. The catalytic role of these conserved regions is strongly supported by locations of residues that are altered in mutants resistant to inhibitors of cytochromeb electron transport.

Key words

Cytochromeb Electron transport Protein evolution Membrane proteins Mitochondria Chloroplasts Protein domains 

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Copyright information

© Springer-Verlag New York Inc. 1989

Authors and Affiliations

  • Neil Howell
    • 1
  1. 1.Division of Research, Department of Radiation TherapyThe University of Texas Medical BranchGalvestonUSA

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