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      The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria

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          Abstract

          Integral proteins in the outer membrane of mitochondria control all aspects of organelle biogenesis, being required for protein import, mitochondrial fission, and, in metazoans, mitochondrial aspects of programmed cell death. How these integral proteins are assembled in the outer membrane had been unclear. In bacteria, Omp85 is an essential component of the protein insertion machinery, and we show that members of the Omp85 protein family are also found in eukaryotes ranging from plants to humans. In eukaryotes, Omp85 is present in the mitochondrial outer membrane. The gene encoding Omp85 is essential for cell viability in yeast, and conditional omp85 mutants have defects that arise from compromised insertion of integral proteins like voltage-dependent anion channel (VDAC) and components of the translocase in the outer membrane of mitochondria (TOM) complex into the mitochondrial outer membrane.

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          Most cited references52

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          Mitochondrial evolution.

          The serial endosymbiosis theory is a favored model for explaining the origin of mitochondria, a defining event in the evolution of eukaryotic cells. As usually described, this theory posits that mitochondria are the direct descendants of a bacterial endosymbiont that became established at an early stage in a nucleus-containing (but amitochondriate) host cell. Gene sequence data strongly support a monophyletic origin of the mitochondrion from a eubacterial ancestor shared with a subgroup of the alpha-Proteobacteria. However, recent studies of unicellular eukaryotes (protists), some of them little known, have provided insights that challenge the traditional serial endosymbiosis-based view of how the eukaryotic cell and its mitochondrion came to be. These data indicate that the mitochondrion arose in a common ancestor of all extant eukaryotes and raise the possibility that this organelle originated at essentially the same time as the nuclear component of the eukaryotic cell rather than in a separate, subsequent event.
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            The hydrogen hypothesis for the first eukaryote.

            A new hypothesis for the origin of eukaryotic cells is proposed, based on the comparative biochemistry of energy metabolism. Eukaryotes are suggested to have arisen through symbiotic association of an anaerobic, strictly hydrogen-dependent, strictly autotrophic archaebacterium (the host) with a eubacterium (the symbiont) that was able to respire, but generated molecular hydrogen as a waste product of anaerobic heterotrophic metabolism. The host's dependence upon molecular hydrogen produced by the symbiont is put forward as the selective principle that forged the common ancestor of eukaryotic cells.
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              CDART: protein homology by domain architecture.

              The Conserved Domain Architecture Retrieval Tool (CDART) performs similarity searches of the NCBI Entrez Protein Database based on domain architecture, defined as the sequential order of conserved domains in proteins. The algorithm finds protein similarities across significant evolutionary distances using sensitive protein domain profiles rather than by direct sequence similarity. Proteins similar to a query protein are grouped and scored by architecture. Relying on domain profiles allows CDART to be fast, and, because it relies on annotated functional domains, informative. Domain profiles are derived from several collections of domain definitions that include functional annotation. Searches can be further refined by taxonomy and by selecting domains of interest. CDART is available at http://www.ncbi.nlm.nih.gov/Structure/lexington/lexington.cgi.
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                Author and article information

                Journal
                J Cell Biol
                The Journal of Cell Biology
                The Rockefeller University Press
                0021-9525
                1540-8140
                5 January 2004
                : 164
                : 1
                : 19-24
                Affiliations
                [1 ]Russell Grimwade School of Biochemistry and Molecular Biology, University of Melbourne, Melbourne 3010, Australia
                [2 ]Centre for Cellular and Molecular Biology, Deakin University, Burwood 3125, Australia
                Author notes

                Address correspondence to Trevor Lithgow, Russell Grimwade School of Biochemistry and Molecular Biology, University of Melbourne, Melbourne 3010, Australia. Tel.: 61-3-8344-4131. Fax: 61-3-9348-2251. email: t.lithgow@ 123456unimelb.edu.au

                Article
                200310092
                10.1083/jcb.200310092
                2171957
                14699090
                4a1fe267-6692-40f2-88b1-c97f40407172
                Copyright © 2004, The Rockefeller University Press
                History
                : 20 October 2003
                : 18 November 2003
                Categories
                Report

                Cell biology
                endosymbiont theory; membrane biogenesis; β-barrel protein; mitochondria; protein import

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