28
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      The mitochondrial import protein Mim1 promotes biogenesis of multispanning outer membrane proteins

      research-article

      Read this article at

      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 Mim1 complex imports α-helical mitochondrial outer membrane proteins with multiple transmembrane segments.

          Abstract

          The mitochondrial outer membrane contains translocase complexes for the import of precursor proteins. The translocase of the outer membrane complex functions as a general preprotein entry gate, whereas the sorting and assembly machinery complex mediates membrane insertion of β-barrel proteins of the outer membrane. Several α-helical outer membrane proteins are known to carry multiple transmembrane segments; however, only limited information is available on the biogenesis of these proteins. We report that mitochondria lacking the mitochondrial import protein 1 (Mim1) are impaired in the biogenesis of multispanning outer membrane proteins, whereas overexpression of Mim1 stimulates their import. The Mim1 complex cooperates with the receptor Tom70 in binding of precursor proteins and promotes their insertion and assembly into the outer membrane. We conclude that the Mim1 complex plays a central role in the import of α-helical outer membrane proteins with multiple transmembrane segments.

          Related collections

          Most cited references51

          • Record: found
          • Abstract: found
          • Article: not found

          Translocation of proteins into mitochondria.

          About 10% to 15% of the nuclear genes of eukaryotic organisms encode mitochondrial proteins. These proteins are synthesized in the cytosol and recognized by receptors on the surface of mitochondria. Translocases in the outer and inner membrane of mitochondria mediate the import and intramitochondrial sorting of these proteins; ATP and the membrane potential are used as energy sources. Chaperones and auxiliary factors assist in the folding and assembly of mitochondrial proteins into their native, three-dimensional structures. This review summarizes the present knowledge on the import and sorting of mitochondrial precursor proteins, with a special emphasis on unresolved questions and topics of current research.
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Common ground for protein translocation: access control for mitochondria and chloroplasts.

            Mitochondria and chloroplasts import the vast majority of their proteins across two membranes, and use translocases of the outer membrane as an entry gate. These translocases interact with the incoming precursor protein and guiding chaperone factors. Within the translocon, precursor-protein receptors dock to a central component that mediates both transfer through a cation-selective channel and initial sorting towards internal subcompartments. Despite these similarities, the mode of translocation differs between the two organelles: in chloroplasts, GTP-binding and hydrolysis by the receptors is required for transport, whereas in mitochondria passage of the preprotein is driven by its increasing affinity for the translocase subunits.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins.

              Mitochondria consist of four compartments-outer membrane, intermembrane space, inner membrane, and matrix--with crucial but distinct functions for numerous cellular processes. A comprehensive characterization of the proteome of an individual mitochondrial compartment has not been reported so far. We used a eukaryotic model organism, the yeast Saccharomyces cerevisiae, to determine the proteome of highly purified mitochondrial outer membranes. We obtained a coverage of approximately 85% based on the known outer membrane proteins. The proteome represents a rich source for the analysis of new functions of the outer membrane, including the yeast homologue (Hfd1/Ymr110c) of the human protein causing Sjögren-Larsson syndrome. Surprisingly, a subclass of proteins known to reside in internal mitochondrial compartments were found in the outer membrane proteome. These seemingly mislocalized proteins included most top scorers of a recent genome-wide analysis for mRNAs that were targeted to mitochondria and coded for proteins of prokaryotic origin. Together with the enrichment of the precursor form of a matrix protein in the outer membrane, we conclude that the mitochondrial outer membrane not only contains resident proteins but also accumulates a conserved subclass of preproteins destined for internal mitochondrial compartments.
                Bookmark

                Author and article information

                Journal
                J Cell Biol
                J. Cell Biol
                jcb
                The Journal of Cell Biology
                The Rockefeller University Press
                0021-9525
                1540-8140
                8 August 2011
                : 194
                : 3
                : 387-395
                Affiliations
                [1 ]Institute for Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research , [2 ]Faculty of Biology , and [3 ]Centre for Biological Signalling Studies, University of Freiburg, 79104 Freiburg, Germany
                [4 ]Abteilung Biophysik, Fachbereich Biologie/Chemie, Universität Osnabrück, 49034 Osnabrück, Germany
                [5 ]Department of Biochemistry and Molecular Biology, Monash University, Melbourne 3800, Australia
                [6 ]Centre de Génétique Moléculaire, Centre National de la Recherche Scientifique, 91190 Gif-sur-Yvette, France
                [7 ]International Institute of Molecular and Cell Biology, 02-109 Warsaw, Poland
                Author notes
                Correspondence to Nikolaus Pfanner: nikolaus.pfanner@ 123456biochemie.uni-freiburg.de
                Article
                201102044
                10.1083/jcb.201102044
                3153637
                21825073
                ebc5eb70-28ec-4ef5-afd1-0205e8440386
                © 2011 Becker et al.

                This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

                History
                : 8 February 2011
                : 11 July 2011
                Categories
                Research Articles
                Report

                Cell biology
                Cell biology

                Comments

                Comment on this article