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      Translocation of Proteins into Mitochondria

      Author(s): 1 , 2
      Publication date Created:
      Publication date (Print):
      Journal: Annual Review of Biochemistry
      Publisher: Annual Reviews

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          Abstract

          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 auxilliary 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.

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          Predotar: A tool for rapidly screening proteomes for N-terminal targeting sequences.

          Ian Small, Nemo Peeters, Fabrice Legeai … (2004)
          Probably more than 25% of the proteins encoded by the nuclear genomes of multicellular eukaryotes are targeted to membrane-bound compartments by N-terminal targeting signals. The major signals are those for the endoplasmic reticulum, the mitochondria, and in plants, plastids. The most abundant of these targeted proteins are well-known and well-studied, but a large proportion remain unknown, including most of those involved in regulation of organellar gene expression or regulation of biochemical pathways. The discovery and characterization of these proteins by biochemical means will be long and difficult. An alternative method is to identify candidate organellar proteins via their characteristic N-terminal targeting sequences. We have developed a neural network-based approach (Predotar--Prediction of Organelle Targeting sequences) for identifying genes encoding these proteins amongst eukaryotic genome sequences. The power of this approach for identifying and annotating novel gene families has been illustrated by the discovery of the pentatricopeptide repeat family.
          Article 0 comments Cited 259 times – based on 0 reviews     Review now
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            Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside.

            Eva Pebay-Peyroula, Cécile Dahout-Gonzalez, Richard Kahn … (2003)
            ATP, the principal energy currency of the cell, fuels most biosynthetic reactions in the cytoplasm by its hydrolysis into ADP and inorganic phosphate. Because resynthesis of ATP occurs in the mitochondrial matrix, ATP is exported into the cytoplasm while ADP is imported into the matrix. The exchange is accomplished by a single protein, the ADP/ATP carrier. Here we have solved the bovine carrier structure at a resolution of 2.2 A by X-ray crystallography in complex with an inhibitor, carboxyatractyloside. Six alpha-helices form a compact transmembrane domain, which, at the surface towards the space between inner and outer mitochondrial membranes, reveals a deep depression. At its bottom, a hexapeptide carrying the signature of nucleotide carriers (RRRMMM) is located. Our structure, together with earlier biochemical results, suggests that transport substrates bind to the bottom of the cavity and that translocation results from a transient transition from a 'pit' to a 'channel' conformation.
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              Predicting subcellular localization of proteins based on their N-terminal amino acid sequence.

              O Emanuelsson, H. Nielsen, S Brunak … (2000)
              A neural network-based tool, TargetP, for large-scale subcellular location prediction of newly identified proteins has been developed. Using N-terminal sequence information only, it discriminates between proteins destined for the mitochondrion, the chloroplast, the secretory pathway, and "other" localizations with a success rate of 85% (plant) or 90% (non-plant) on redundancy-reduced test sets. From a TargetP analysis of the recently sequenced Arabidopsis thaliana chromosomes 2 and 4 and the Ensembl Homo sapiens protein set, we estimate that 10% of all plant proteins are mitochondrial and 14% chloroplastic, and that the abundance of secretory proteins, in both Arabidopsis and Homo, is around 10%. TargetP also predicts cleavage sites with levels of correctly predicted sites ranging from approximately 40% to 50% (chloroplastic and mitochondrial presequences) to above 70% (secretory signal peptides). TargetP is available as a web-server at http://www.cbs.dtu.dk/services/TargetP/. Copyright 2000 Academic Press.
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                Author and article information

                Journal
                Title: Annual Review of Biochemistry
                Abbreviated Title: Annu. Rev. Biochem.
                Publisher: Annual Reviews
                ISSN (Print): 0066-4154
                ISSN (Electronic): 1545-4509
                Publication date Created: June 07 2007
                Publication date (Print): June 07 2007
                Volume: 76
                Issue: 1
                Pages: 723-749
                Affiliations
                [1 ]Institut für Physiologische Chemie, Universität München, 81377 München, Germany;
                [2 ]Institut für Zellbiologie, Universität Kaiserslautern, 67663 Kaiserslautern, Germany;
                Article
                DOI: 10.1146/annurev.biochem.76.052705.163409
                PubMed ID: 17263664
                SO-VID: 3e29ee28-b860-459c-bcdd-f52337ee06eb
                Copyright © © 2007
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