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Thomas, Douglas D.

Biological Chemistry

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Volume 392, Issue 1-2 (Feb 2011)


Evolution of YidC/Oxa1/Alb3 insertases: three independent gene duplications followed by functional specialization in bacteria, mitochondria and chloroplasts

Soledad Funes
  • Departamento de Genética Molecular, Instituto de Fisiología Celular, Circuito Exterior s/n, Ciudad Universitaria, Universidad Nacional Autónoma de México, Mexico D.F. 04510, Mexico
/ Frank Kauff
  • Molecular Phylogenetics, University of Kaiserslautern, Erwin-Schroedinger-Strasse 13, D-67663 Kaiserslautern, Germany
/ Eli O. van der Sluis
  • Gene Center, University of Munich, Feodor-Lynen-Strasse 25, D-81337 Munich, Germany
/ Martin Ott
  • Membrane Biogenesis, University of Kaiserslautern, Erwin-Schroedinger-Strasse 13, D-67663 Kaiserslautern, Germany
/ Johannes M. Herrmann
  • Cell Biology, University of Kaiserslautern, Erwin-Schroedinger-Strasse 13, D-67663 Kaiserslautern, Germany
  • Email:
Published Online: 2011-06-18 | DOI: https://doi.org/10.1515/bc.2011.013


Members of the YidC/Oxa1/Alb3 protein family facilitate the insertion, folding and assembly of proteins of the inner membranes of bacteria and mitochondria and the thylakoid membrane of plastids. All homologs share a conserved hydrophobic core region comprising five transmembrane domains. On the basis of phylogenetic analyses, six subgroups of the family can be distinguished which presumably arose from three independent gene duplications followed by functional specialization. During evolution of bacteria, mitochondria and chloroplasts, subgroup-specific regions were added to the core domain to facilitate the association with ribosomes or other components contributing to the substrate spectrum of YidC/Oxa1/Alb3 proteins.

Keywords: complex assembly; membrane biogenesis; protein evolution; protein folding; respiratory chain

About the article

Corresponding author

Received: 2010-07-26

Accepted: 2010-10-20

Published Online: 2011-06-18

Published in Print: 2011-02-01

Citation Information: Biological Chemistry, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/bc.2011.013. Export Citation

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