Structure of the mitochondrial import gate reveals distinct preprotein paths.

Cryoelectron Microscopy Mitochondria / chemistry Mitochondrial Membrane Transport Proteins / chemistry Mitochondrial Precursor Protein Import Complex Proteins Models, Molecular Phospholipids / metabolism Protein Multimerization Saccharomyces cerevisiae / chemistry Saccharomyces cerevisiae Proteins / chemistry

Journal

Nature
ISSN: 1476-4687
Titre abrégé: Nature
Pays: England
ID NLM: 0410462

Informations de publication

Date de publication:
11 2019
Historique:
received: 17 03 2019
accepted: 30 09 2019
pubmed: 11 10 2019
medline: 24 3 2020
entrez: 11 10 2019
Statut: ppublish

Résumé

The translocase of the outer mitochondrial membrane (TOM) is the main entry gate for proteins

Identifiants

DOI: 10.1038/s41586-019-1680-7 PMID: 31600774
pubmed: 31600774
doi: 10.1038/s41586-019-1680-7
pii: 10.1038/s41586-019-1680-7
doi:

Substances chimiques

MIA40 protein, S cerevisiae 0
Mitochondrial Membrane Transport Proteins 0
Mitochondrial Precursor Protein Import Complex Proteins 0
Phospholipids 0
Saccharomyces cerevisiae Proteins 0
TOM5 protein, S cerevisiae 0
TOM6 protein, S cerevisiae 0
Tom40 protein, S cerevisiae 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

395-401

Subventions

Organisme : European Research Council
Pays : International

Références

Endo, T. & Yamano, K. Multiple pathways for mitochondrial protein traffic. Biol. Chem. 390, 723–730 (2009).
doi: 10.1515/BC.2009.087 pubmed: 19453276
Neupert, W. A perspective on transport of proteins into mitochondria: a myriad of open questions. J. Mol. Biol. 427, 1135–1158 (2015).
doi: 10.1016/j.jmb.2015.02.001 pubmed: 25676309
Pfanner, N., Warscheid, B. & Wiedemann, N. Mitochondrial proteins: from biogenesis to functional networks. Nat. Rev. Mol. Cell Biol. 20, 267–284 (2019).
doi: 10.1038/s41580-018-0092-0 pubmed: 30626975 pmcid: 6684368
Shiota, T. et al. Molecular architecture of the active mitochondrial protein gate. Science 349, 1544–1548 (2015).
doi: 10.1126/science.aac6428 pubmed: 26404837
Sakaue, H. et al. Porin associates with Tom22 to regulate the mitochondrial protein gate assembly. Mol. Cell 73, 1044–1055 (2019).
doi: 10.1016/j.molcel.2019.01.003 pubmed: 30738703
Künkele, K.-P. et al. The preprotein translocation channel of the outer membrane of mitochondria. Cell 93, 1009–1019 (1998).
doi: 10.1016/S0092-8674(00)81206-4 pubmed: 9635430
Ahting, U. et al. The TOM core complex: the general protein import pore of the outer membrane of mitochondria. J. Cell Biol. 147, 959–968 (1999).
doi: 10.1083/jcb.147.5.959 pubmed: 10579717 pmcid: 2169338
Model, K., Meisinger, C. & Kühlbrandt, W. Cryo-electron microscopy structure of a yeast mitochondrial preprotein translocase. J. Mol. Biol. 383, 1049–1057 (2008).
doi: 10.1016/j.jmb.2008.07.087 pubmed: 18706915
Bausewein, T. et al. Cryo-EM structure of the TOM core complex from Neurospora crassa. Cell 170, 693–700 (2017).
doi: 10.1016/j.cell.2017.07.012 pubmed: 28802041
Van den Berg, B. et al. X-ray structure of a protein-conducting channel. Nature 427, 36–44 (2004).
doi: 10.1038/nature02218 pubmed: 14661030
Voorhees, R. M., Fernández, I. S., Scheres, S. H. W. & Hegde, R. S. Structure of the mammalian ribosome–Sec61 complex to 3.4 Å resolution. Cell 157, 1632–1643 (2014).
doi: 10.1016/j.cell.2014.05.024 pubmed: 24930395 pmcid: 4081569
Gogala, M. et al. Structures of the Sec61 complex engaged in nascent peptide translocation or membrane insertion. Nature 506, 107–110 (2014).
doi: 10.1038/nature12950 pubmed: 24499919
Itskanov, S. & Park, E. Structure of the posttranslational Sec protein–translocation channel complex from yeast. Science 363, 84–87 (2019).
doi: 10.1126/science.aav6740 pubmed: 30545845
Wu, X., Cabanos, C. & Rapoport, T. A. Structure of the post-translational protein translocation machinery of the ER membrane. Nature 566, 136–139 (2019).
doi: 10.1038/s41586-018-0856-x pubmed: 30644436
Baud, C. et al. Translocation path of a substrate protein through its Omp85 transporter. Nat. Commun. 5, 5271 (2014).
doi: 10.1038/ncomms6271 pubmed: 25327833
Lundquist, K., Bakelar, J., Noinaj, N. & Gumbart, J. C. C-terminal kink formation is required for lateral gating in BamA. Proc. Natl Acad. Sci. USA 115, E7942–E7949 (2018).
doi: 10.1073/pnas.1722530115 pubmed: 30087180
Bamert, R. S. et al. Structural basis for substrate selection by the translocation and assembly module of the β-barrel assembly machinery. Mol. Microbiol. 106, 142–156 (2017).
doi: 10.1111/mmi.13757 pubmed: 28752534 pmcid: 5607099
Model, K. et al. Protein translocase of the outer mitochondrial membrane: role of import receptors in the structural organization of the TOM complex. J. Mol. Biol. 316, 657–666 (2002).
doi: 10.1006/jmbi.2001.5365 pubmed: 11866524
Dolezal, P., Likic, V., Tachezy, J. & Lithgow, T. Evolution of the molecular machines for protein import into mitochondria. Science 313, 314–318 (2006).
doi: 10.1126/science.1127895 pubmed: 16857931
Fukasawa, Y., Oda, T., Tomii, K. & Imai, K. Origin and evolutionary alteration of the mitochondrial import system in eukaryotic lineages. Mol. Biol. Evol. 34, 1574–1586 (2017).
doi: 10.1093/molbev/msx096 pubmed: 28369657 pmcid: 5455965
Maćasev, D. et al. Tom22′, an 8-kDa trans-site receptor in plants and protozoans, is a conserved feature of the TOM complex that appeared early in the evolution of eukaryotes. Mol. Biol. Evol. 21, 1557–1564 (2004).
doi: 10.1093/molbev/msh166 pubmed: 15155803
Senes, A., Gerstein, M. & Engelman, D. M. Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with β-branched residues at neighboring positions. J. Mol. Biol. 296, 921–936 (2000).
doi: 10.1006/jmbi.1999.3488 pubmed: 10677292
Harner, M., Neupert, W. & Deponte, M. Lateral release of proteins from the TOM complex into the outer membrane of mitochondria. EMBO J. 30, 3232–3241 (2011).
doi: 10.1038/emboj.2011.235 pubmed: 21765393 pmcid: 3160657
Höhr, A. I. C. et al. Membrane protein insertion through a mitochondrial β-barrel gate. Science 359, eaah6834 (2018).
doi: 10.1126/science.aah6834 pubmed: 29348211 pmcid: 5959003
Yamano, K., Tanaka-Yamano, S. & Endo, T. Tom7 regulates Mdm10-mediated assembly of the mitochondrial import channel protein Tom40. J. Biol. Chem. 285, 41222–41231 (2010).
doi: 10.1074/jbc.M110.163238 pubmed: 21036907 pmcid: 3009848
Ellenrieder, L. et al. Separating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of Mdm10. Nat. Commun. 7, 13021 (2016).
doi: 10.1038/ncomms13021 pubmed: 27721450 pmcid: 5476798
Esaki, M. et al. Mitochondrial protein import. Requirement of presequence elements and TOM components for precursor binding to the TOM complex. J. Biol. Chem. 279, 45701–45707 (2004).
doi: 10.1074/jbc.M404591200 pubmed: 15337763
Court, D. A. et al. Role of the intermembrane-space domain of the preprotein receptor Tom22 in protein import into mitochondria. Mol. Cell. Biol. 16, 4035–4042 (1996).
doi: 10.1128/MCB.16.8.4035 pubmed: 8754801 pmcid: 231399
Moczko, M. et al. The intermembrane space domain of mitochondrial Tom22 functions as a trans binding site for preproteins with N-terminal targeting sequences. Mol. Cell. Biol. 17, 6574–6584 (1997).
doi: 10.1128/MCB.17.11.6574 pubmed: 9343421 pmcid: 232511
Kanamori, T. et al. Uncoupling of transfer of the presequence and unfolding of the mature domain in precursor translocation across the mitochondrial outer membrane. Proc. Natl Acad. Sci. USA 96, 3634–3639 (1999).
doi: 10.1073/pnas.96.7.3634 pubmed: 10097089
Rapaport, D., Neupert, W. & Lill, R. Mitochondrial protein import. Tom40 plays a major role in targeting and translocation of preproteins by forming a specific binding site for the presequence. J. Biol. Chem. 272, 18725–18731 (1997).
doi: 10.1074/jbc.272.30.18725 pubmed: 9228044
Yamamoto, H. et al. Tim50 is a subunit of the TIM23 complex that links protein translocation across the outer and inner mitochondrial membranes. Cell 111, 519–528 (2002).
doi: 10.1016/S0092-8674(02)01053-X pubmed: 12437925
Mokranjac, D. et al. Tim50, a novel component of the TIM23 preprotein translocase of mitochondria. EMBO J. 22, 816–825 (2003).
doi: 10.1093/emboj/cdg090 pubmed: 12574118 pmcid: 145450
Shiota, T., Mabuchi, H., Tanaka-Yamano, S., Yamano, K. & Endo, T. In vivo protein-interaction mapping of a mitochondrial translocator protein Tom22 at work. Proc. Natl Acad. Sci. USA 108, 15179–15183 (2011).
doi: 10.1073/pnas.1105921108 pubmed: 21896724
Tamura, Y. et al. Tim23–Tim50 pair coordinates functions of translocators and motor proteins in mitochondrial protein import. J. Cell Biol. 184, 129–141 (2009).
doi: 10.1083/jcb.200808068 pubmed: 19139266 pmcid: 2615085
Chacinska, A. et al. Mitochondrial presequence translocase: switching between TOM tethering and motor recruitment involves Tim21 and Tim17. Cell 120, 817–829 (2005).
doi: 10.1016/j.cell.2005.01.011 pubmed: 15797382
Naoé, M. et al. Identification of Tim40 that mediates protein sorting to the mitochondrial intermembrane space. J. Biol. Chem. 279, 47815–47821 (2004).
doi: 10.1074/jbc.M410272200 pubmed: 15364952
Gornicka, A. et al. A discrete pathway for the transfer of intermembrane space proteins across the outer membrane of mitochondria. Mol. Biol. Cell 25, 3999–4009 (2014).
doi: 10.1091/mbc.e14-06-1155 pubmed: 25318675 pmcid: 4263444
Chacinska, A. et al. Essential role of Mia40 in import and assembly of mitochondrial intermembrane space proteins. EMBO J. 23, 3735–3746 (2004).
doi: 10.1038/sj.emboj.7600389 pubmed: 15359280 pmcid: 522791
Mesecke, N. et al. A disulfide relay system in the intermembrane space of mitochondria that mediates protein import. Cell 121, 1059–1069 (2005).
doi: 10.1016/j.cell.2005.04.011 pubmed: 15989955
Kurz, M. Martin, H. Rassow, J., Pfanner, N. & Ryan, M. T. Biogenesis of Tim proteins of the mitochondrial carrier pathway: differential targeting mechanisms and crossing over with the main import pathway. Mol. Biol. Cell 10, 2461–2474 (1999).
doi: 10.1091/mbc.10.7.2461 pubmed: 10397776 pmcid: 25469
Stojanovski, D. et al. Mitochondrial protein import: precursor oxidation in a ternary complex with disulfide carrier and sulfhydryl oxidase. J. Cell Biol. 183, 195–202 (2008).
doi: 10.1083/jcb.200804095 pubmed: 18852299 pmcid: 2568017
Bien, M. et al. Mitochondrial disulfide bond formation is driven by intersubunit electron transfer in Erv1 and proofread by glutathione. Mol. Cell 37, 516–528 (2010).
doi: 10.1016/j.molcel.2010.01.017 pubmed: 20188670
Rapaport, D. et al. Structural requirements of Tom40 for assembly into preexisting TOM complexes of mitochondria. Mol. Biol. Cell 12, 1189–1198 (2001).
doi: 10.1091/mbc.12.5.1189 pubmed: 11359915 pmcid: 34577
Habich, M. et al. Vectorial import via a metastable disulfide-linked complex allows for a quality control step and import by the mitochondrial disulfide relay. Cell Rep. 26, 759–774 (2019).
doi: 10.1016/j.celrep.2018.12.092 pubmed: 30650365
Becker, T. et al. Role of phosphatidylethanolamine in the biogenesis of mitochondrial outer membrane proteins. J. Biol. Chem. 288, 16451–16459 (2013).
doi: 10.1074/jbc.M112.442392 pubmed: 23625917 pmcid: 3675581
Zheng, W. et al. Adaptive optics improves multiphoton super-resolution imaging. Nat. Methods 14, 869–872 (2017).
doi: 10.1038/nmeth.4337 pubmed: 28628128
Rohou, A. & Grigorieff, N. CTFFIND4: Fast and accurate defocus estimation from electron micrographs. J. Struct. Biol. 192, 216–221 (2015).
doi: 10.1016/j.jsb.2015.08.008 pubmed: 26278980 pmcid: 6760662
Zivanov, J. et al. New tools for automated high-resolution cryo-EM structure determination in RELION-3. eLife 7, e42166 (2018).
doi: 10.7554/eLife.42166 pubmed: 30412051 pmcid: 6250425
Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D 66, 486–501 (2010).
doi: 10.1107/S0907444910007493
Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66, 213–221 (2010).
doi: 10.1107/S0907444909052925 pubmed: 20124702
Pettersen, E. F. et al. UCSF Chimera—a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605–1612 (2004).
doi: 10.1002/jcc.20084
Sikorski, R. S. & Hieter, P. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19–27 (1989).
pubmed: 2659436 pmcid: 1203683
Model, K. et al. Multistep assembly of the protein import channel of the mitochondrial outer membrane. Nat. Struct. Biol. 8, 361–370 (2001).
doi: 10.1038/86253 pubmed: 11276259
Opaliński, Ł. et al. Recruitment of cytosolic J-proteins by TOM receptors promotes mitochondrial protein biogenesis. Cell Rep. 25, 2036–2043 (2018).
doi: 10.1016/j.celrep.2018.10.083 pubmed: 30463002 pmcid: 6280124
Qiu, J. et al. Coupling of mitochondrial import and export translocases by receptor-mediated supercomplex formation. Cell 154, 596–608 (2013).
doi: 10.1016/j.cell.2013.06.033 pubmed: 23911324
Ando, T., Uchihashi, T. & Fukuma, T. High-speed atomic force microscopy for nano-visualization of dynamic biomolecular processes. Prog. Surf. Sci. 83, 337–437 (2008).
doi: 10.1016/j.progsurf.2008.09.001
Uchihashi, T., Kodera, N. & Ando, T. Guide to video recording of structure dynamics and dynamic processes of proteins by high-speed atomic force microscopy. Nat. Protoc. 7, 1193–1206 (2012).
doi: 10.1038/nprot.2012.047 pubmed: 22635111
Milenkovic, D. et al. Identification of the signal directing Tim9 and Tim10 into the intermembrane space of mitochondria. Mol. Biol. Cell 20, 2530–2539 (2009).
doi: 10.1091/mbc.e08-11-1108 pubmed: 19297525 pmcid: 2682594
Thornton, N. et al. Two modular forms of the mitochondrial sorting and assembly machinery are involved in biogenesis of α-helical outer membrane proteins. J. Mol. Biol. 396, 540–549 (2010).
doi: 10.1016/j.jmb.2009.12.026 pubmed: 20026336
Katoh, K. & Standley, D. M. MAFFT multiple sequence alignment software version 7: improvements in performance and usability. Mol. Biol. Evol. 30, 772–780 (2013).
doi: 10.1093/molbev/mst010 pubmed: 23329690 pmcid: 23329690
Waterhouse, A. M., Procter, J. B., Martin, D. M. A., Clamp, M. & Barton, G. J. Jalview Version 2—a multiple sequence alignment editor and analysis workbench. Bioinformatics 25, 1189–1191 (2009).
doi: 10.1093/bioinformatics/btp033 pubmed: 19151095 pmcid: 2672624
Ashkenazy, H. et al. ConSurf 2016: an improved methodology to estimate and visualize evolutionary conservation in macromolecules. Nucleic Acids Res. 44, W344–W350 (2016).
doi: 10.1093/nar/gkw408 pubmed: 27166375 pmcid: 4987940

Auteurs

Yuhei Araiso (Y)

Faculty of Life Sciences, Kyoto Sangyo University, Kyoto, Japan.
Institute for Protein Dynamics, Kyoto Sangyo University, Kyoto, Japan.
Department of Clinical Laboratory Science, Division of Health Sciences, Graduate School of Medical Science, Kanazawa University, Kanazawa, Japan.

Akihisa Tsutsumi (A)

Department of Cell Biology and Anatomy, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.

Jian Qiu (J)

Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
Spemann Graduate School of Biology and Medicine, University of Freiburg, Freiburg, Germany.
Institute of Molecular Precision Medicine and Hunan Key Laboratory of Molecular Precision Medicine, Xiangya Hospital, Central South University, Changsha, China.

Kenichiro Imai (K)

Molecular Profiling Research Center for Drug Discovery (molprof), National Institute of Advanced Industrial Science and Technology (AIST), Tokyo, Japan.

Takuya Shiota (T)

Infection and Immunity Program, Biomedicine Discovery Institute and Department of Microbiology, Monash University, Melbourne, Victoria, Australia.
Organization for Promotion of Tenure Track, University of Miyazaki, Miyazaki, Japan.

Jiyao Song (J)

Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.

Caroline Lindau (C)

Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
Faculty of Biology, University of Freiburg, Freiburg, Germany.

Lena-Sophie Wenz (LS)

Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
Sanofi Deutschland, Frankfurt am Main, Germany.

Haruka Sakaue (H)

Faculty of Life Sciences, Kyoto Sangyo University, Kyoto, Japan.
Institute for Protein Dynamics, Kyoto Sangyo University, Kyoto, Japan.

Kaori Yunoki (K)

Faculty of Life Sciences, Kyoto Sangyo University, Kyoto, Japan.

Shin Kawano (S)

Faculty of Life Sciences, Kyoto Sangyo University, Kyoto, Japan.
Institute for Protein Dynamics, Kyoto Sangyo University, Kyoto, Japan.

Junko Suzuki (J)

Faculty of Life Sciences, Kyoto Sangyo University, Kyoto, Japan.

Marilena Wischnewski (M)

Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
Swiss Federal Institute of Technology (EPFL), Lausanne, Switzerland.

Conny Schütze (C)

Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.

Hirotaka Ariyama (H)

Nano Life Science Institute (WPI-Nano LSI), Kanazawa University, Kanazawa, Japan.

Toshio Ando (T)

Nano Life Science Institute (WPI-Nano LSI), Kanazawa University, Kanazawa, Japan.

Thomas Becker (T)

Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
CIBSS Centre for Integrative Biological Signalling Studies, University of Freiburg, Freiburg, Germany.

Trevor Lithgow (T)

Infection and Immunity Program, Biomedicine Discovery Institute and Department of Microbiology, Monash University, Melbourne, Victoria, Australia.

Nils Wiedemann (N)

Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
CIBSS Centre for Integrative Biological Signalling Studies, University of Freiburg, Freiburg, Germany.

Nikolaus Pfanner (N)

Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
CIBSS Centre for Integrative Biological Signalling Studies, University of Freiburg, Freiburg, Germany.

Masahide Kikkawa (M)

Department of Cell Biology and Anatomy, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.

Toshiya Endo (T)

Faculty of Life Sciences, Kyoto Sangyo University, Kyoto, Japan. tendo@cc.kyoto-su.ac.jp.
Institute for Protein Dynamics, Kyoto Sangyo University, Kyoto, Japan. tendo@cc.kyoto-su.ac.jp.

Articles similaires

Atomic view of photosynthetic metabolite permeability pathways and confinement in synthetic carboxysome shells.

Daipayan Sarkar, Christopher Maffeo, Markus Sutter et al.
1.00
Photosynthesis Ribulose-Bisphosphate Carboxylase Carbon Dioxide Molecular Dynamics Simulation Cyanobacteria

Pathogenic mitochondrial DNA mutations inhibit melanoma metastasis.

Spencer D Shelton, Sara House, Luiza Martins Nascentes Melo et al.
1.00
DNA, Mitochondrial Humans Melanoma Mutation Neoplasm Metastasis

A dual role for PSIP1/LEDGF in T cell acute lymphoblastic leukemia.

Lisa Demoen, Filip Matthijssens, Lindy Reunes et al.
1.00
Precursor T-Cell Lymphoblastic Leukemia-Lymphoma Animals Mice Humans Cell Line, Tumor

Mouse α-synuclein fibrils are structurally and functionally distinct from human fibrils associated with Lewy body diseases.

Arpine Sokratian, Ye Zhou, Meltem Tatli et al.
1.00
alpha-Synuclein Humans Animals Mice Lewy Body Disease

Classifications MeSH

questionsmedicales.fr › Techniques d'investigation › Microscopie électronique › Cryomicroscopie électronique › Structure of the mitochondrial import gate...
questionsmedicales.fr › Cellules › Structures cellulaires › Fractions subcellulaires › Mitochondries › Structure of the mitochondrial import gate...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines mitochondriales › Protéines de transport de la membrane mitochondriale › Structure of the mitochondrial import gate...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines mitochondriales › Protéines de transport de la membrane mitochondriale › Protéines du complexe d'import des protéines précurseurs mitochondriales › Structure of the mitochondrial import gate...
questionsmedicales.fr › Techniques d'investigation › Modèles théoriques › Modèles moléculaires › Structure of the mitochondrial import gate...
questionsmedicales.fr › Lipides › Lipides membranaires › Phospholipides › Structure of the mitochondrial import gate...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Multimérisation de protéines › Structure of the mitochondrial import gate...
questionsmedicales.fr › Eucaryotes › Champignons › Levures › Saccharomyces › Saccharomyces cerevisiae › Structure of the mitochondrial import gate...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines fongiques › Protéines de Saccharomyces cerevisiae › Structure of the mitochondrial import gate...