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  1. Article ; Online: Global analysis of the mitochondrial N-proteome identifies a processing peptidase critical for protein stability.

    Vögtle, F-Nora / Wortelkamp, Stefanie / Zahedi, René P / Becker, Dorothea / Leidhold, Claudia / Gevaert, Kris / Kellermann, Josef / Voos, Wolfgang / Sickmann, Albert / Pfanner, Nikolaus / Meisinger, Chris

    Cell

    2009  Volume 139, Issue 2, Page(s) 428–439

    Abstract: Many mitochondrial proteins are synthesized with N-terminal presequences that are removed ... by specific peptidases. The N-termini of the mature proteins and thus peptidase cleavage sites have only been ... analysis of the N-proteome of yeast mitochondria, revealing the N-termini of 615 different proteins ...

    Abstract Many mitochondrial proteins are synthesized with N-terminal presequences that are removed by specific peptidases. The N-termini of the mature proteins and thus peptidase cleavage sites have only been determined for a small fraction of mitochondrial proteins and yielded a controversial situation for the cleavage site specificity of the major mitochondrial processing peptidase (MPP). We report a global analysis of the N-proteome of yeast mitochondria, revealing the N-termini of 615 different proteins. Significantly more proteins than predicted contained cleavable presequences. We identified the intermediate cleaving peptidase Icp55, which removes an amino acid from a characteristic set of MPP-generated N-termini, solving the controversial situation of MPP specificity and suggesting that Icp55 converts instable intermediates into stable proteins. Our results suggest that Icp55 is critical for stabilization of the mitochondrial proteome and illustrate how the N-proteome can serve as rich source for a systematic analysis of mitochondrial protein targeting, cleavage and turnover.
    MeSH term(s) Humans ; Mitochondria/chemistry ; Mitochondrial Proteins/analysis ; Peptide Hydrolases/metabolism ; Protein Stability ; Proteome/analysis ; Saccharomyces cerevisiae/chemistry
    Chemical Substances Mitochondrial Proteins ; Proteome ; Peptide Hydrolases (EC 3.4.-)
    Language English
    Publishing date 2009-10-16
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2009.07.045
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  2. Article ; Online: Mitochondrial entry gate as regulatory hub.

    den Brave, Fabian / Pfanner, Nikolaus / Becker, Thomas

    Biochimica et biophysica acta. Molecular cell research

    2023  Volume 1871, Issue 2, Page(s) 119529

    Abstract: Mitochondria import 1000-1300 different precursor proteins from the cytosol. The main mitochondrial entry gate is formed by the translocase of the outer membrane (TOM complex). Molecular coupling and modification of TOM subunits control and modulate ... ...

    Abstract Mitochondria import 1000-1300 different precursor proteins from the cytosol. The main mitochondrial entry gate is formed by the translocase of the outer membrane (TOM complex). Molecular coupling and modification of TOM subunits control and modulate protein import in response to cellular signaling. The TOM complex functions as regulatory hub to integrate mitochondrial protein biogenesis and quality control into the cellular proteostasis network.
    MeSH term(s) Mitochondrial Precursor Protein Import Complex Proteins ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Saccharomyces cerevisiae/metabolism ; Mitochondria/metabolism ; Mitochondrial Membranes/metabolism
    Chemical Substances Mitochondrial Precursor Protein Import Complex Proteins ; Mitochondrial Proteins
    Language English
    Publishing date 2023-11-09
    Publishing country Netherlands
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 60-7
    ISSN 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbamcr.2023.119529
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Morpholinos meet mitochondria: Targeting organellar gene expression.

    Rampelt, Heike / Pfanner, Nikolaus

    Cell

    2021  Volume 184, Issue 23, Page(s) 5693–5695

    Abstract: The mitochondrial genome encodes proteins central to mitochondrial function; however, transcript-specific mechanistic studies of mitochondrial gene products have been difficult because of challenges in their experimental manipulation. Cruz-Zaragoza et al. ...

    Abstract The mitochondrial genome encodes proteins central to mitochondrial function; however, transcript-specific mechanistic studies of mitochondrial gene products have been difficult because of challenges in their experimental manipulation. Cruz-Zaragoza et al. provide a solution to this challenge, introducing an elegant system for efficient translational silencing of transcripts in human mitochondria.
    MeSH term(s) Gene Expression ; Humans ; Mitochondria/genetics ; Mitochondrial Proteins/genetics ; Morpholinos ; Organelles
    Chemical Substances Mitochondrial Proteins ; Morpholinos
    Language English
    Publishing date 2021-11-10
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2021.10.019
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  4. Article ; Online: Mitochondrial protein transport: Versatility of translocases and mechanisms.

    Busch, Jakob D / Fielden, Laura F / Pfanner, Nikolaus / Wiedemann, Nils

    Molecular cell

    2023  Volume 83, Issue 6, Page(s) 890–910

    Abstract: Biogenesis of mitochondria requires the import of approximately 1,000 different precursor proteins into and across the mitochondrial membranes. Mitochondria exhibit a wide variety of mechanisms and machineries for the translocation and sorting of ... ...

    Abstract Biogenesis of mitochondria requires the import of approximately 1,000 different precursor proteins into and across the mitochondrial membranes. Mitochondria exhibit a wide variety of mechanisms and machineries for the translocation and sorting of precursor proteins. Five major import pathways that transport proteins to their functional intramitochondrial destination have been elucidated; these pathways range from the classical amino-terminal presequence-directed pathway to pathways using internal or even carboxy-terminal targeting signals in the precursors. Recent studies have provided important insights into the structural organization of membrane-embedded preprotein translocases of mitochondria. A comparison of the different translocases reveals the existence of at least three fundamentally different mechanisms: two-pore-translocase, β-barrel switching, and transport cavities open to the lipid bilayer. In addition, translocases are physically engaged in dynamic interactions with respiratory chain complexes, metabolite transporters, quality control factors, and machineries controlling membrane morphology. Thus, mitochondrial preprotein translocases are integrated into multi-functional networks of mitochondrial and cellular machineries.
    MeSH term(s) Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Mitochondria/genetics ; Mitochondria/metabolism ; Mitochondrial Membranes/metabolism ; Carrier Proteins/metabolism ; Protein Transport ; Protein Precursors/metabolism ; Mitochondrial Membrane Transport Proteins/genetics ; Mitochondrial Membrane Transport Proteins/metabolism
    Chemical Substances Mitochondrial Proteins ; Carrier Proteins ; Protein Precursors ; Mitochondrial Membrane Transport Proteins
    Language English
    Publishing date 2023-03-16
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2023.02.020
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  5. Article: The intermembrane space domain of mitochondrial Tom22 functions as a trans binding site for preproteins with N-terminal targeting sequences.

    Moczko, M / Bömer, U / Kübrich, M / Zufall, N / Hönlinger, A / Pfanner, N

    Molecular and cellular biology

    1997  Volume 17, Issue 11, Page(s) 6574–6584

    Abstract: ... that a lack of the IMS domain only moderately reduces the direct import of preproteins with N-terminal ... of Tom22 functions as a trans binding site for preproteins with N-terminal targeting sequences ...

    Abstract Mitochondrial protein import is thought to involve the sequential interaction of preproteins with binding sites on cis and trans sides of the membranes. For translocation across the outer membrane, preproteins first interact with the cytosolic domains of import receptors (cis) and then are translocated through a general import pore, in a process proposed to involve binding to a trans site on the intermembrane space (IMS) side. Controversial results have been reported for the role of the IMS domain of the essential outer membrane protein Tom22 in formation of the trans site. We show with different mutant mitochondria that a lack of the IMS domain only moderately reduces the direct import of preproteins with N-terminal targeting sequences. The dependence of import on the IMS domain of Tom22 is significantly enhanced by removing the cytosolic domains of import receptors or by performing import in two steps, i.e., accumulation of a preprotein at the outer membrane in the absence of a membrane potential (delta psi) and subsequent import after reestablishment of a delta psi. After the removal of cytosolic receptor domains, two-step import of a cleavable preprotein strictly requires the IMS domain. In contrast, preproteins with internal targeting information do not depend on the IMS domain of Tom22. We conclude that the negatively charged IMS domain of Tom22 functions as a trans binding site for preproteins with N-terminal targeting sequences, in agreement with the acid chain hypothesis of mitochondrial protein import.
    MeSH term(s) Biological Transport ; Cell Compartmentation ; Intracellular Membranes/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Membrane Transport Proteins ; Mitochondria/metabolism ; Mitochondrial Membrane Transport Proteins ; Protein Binding ; Protein Conformation ; Protein Precursors/metabolism ; Protein Sorting Signals/metabolism ; Proton-Motive Force ; Receptors, Cell Surface ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins ; Sequence Deletion ; Tetrahydrofolate Dehydrogenase/metabolism
    Chemical Substances Membrane Proteins ; Membrane Transport Proteins ; Mitochondrial Membrane Transport Proteins ; Protein Precursors ; Protein Sorting Signals ; Receptors, Cell Surface ; Saccharomyces cerevisiae Proteins ; TOM22 protein, S cerevisiae ; Tetrahydrofolate Dehydrogenase (EC 1.5.1.3)
    Language English
    Publishing date 1997-11
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 779397-2
    ISSN 1098-5549 ; 0270-7306
    ISSN (online) 1098-5549
    ISSN 0270-7306
    DOI 10.1128/MCB.17.11.6574
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  6. Article ; Online: Author Correction: Mitochondrial proteins: from biogenesis to functional networks.

    Pfanner, Nikolaus / Warscheid, Bettina / Wiedemann, Nils

    Nature reviews. Molecular cell biology

    2021  Volume 22, Issue 5, Page(s) 367

    Language English
    Publishing date 2021-04-27
    Publishing country England
    Document type Published Erratum
    ZDB-ID 2031313-5
    ISSN 1471-0080 ; 1471-0072
    ISSN (online) 1471-0080
    ISSN 1471-0072
    DOI 10.1038/s41580-021-00361-x
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  7. Article ; Online: Mitochondrial complexome and import network.

    den Brave, Fabian / Schulte, Uwe / Fakler, Bernd / Pfanner, Nikolaus / Becker, Thomas

    Trends in cell biology

    2023  

    Abstract: Mitochondria perform crucial functions in cellular metabolism, protein and lipid biogenesis, quality control, and signaling. The systematic analysis of protein complexes and interaction networks provided exciting insights into the structural and ... ...

    Abstract Mitochondria perform crucial functions in cellular metabolism, protein and lipid biogenesis, quality control, and signaling. The systematic analysis of protein complexes and interaction networks provided exciting insights into the structural and functional organization of mitochondria. Most mitochondrial proteins do not act as independent units, but are interconnected by stable or dynamic protein-protein interactions. Protein translocases are responsible for importing precursor proteins into mitochondria and form central elements of several protein interaction networks. These networks include molecular chaperones and quality control factors, metabolite channels and respiratory chain complexes, and membrane and organellar contact sites. Protein translocases link the distinct networks into an overarching network, the mitochondrial import network (MitimNet), to coordinate biogenesis, membrane organization and function of mitochondria.
    Language English
    Publishing date 2023-10-30
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 30122-x
    ISSN 1879-3088 ; 0962-8924
    ISSN (online) 1879-3088
    ISSN 0962-8924
    DOI 10.1016/j.tcb.2023.10.004
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  8. Article ; Online: Mitochondria and friends - a special issue in honor of Walter Neupert (1939-2019).

    Herrmann, Johannes M / Hartl, F Ulrich / Pfanner, Nikolaus

    Biological chemistry

    2020  Volume 401, Issue 6-7, Page(s) 643–644

    MeSH term(s) Biochemistry/history ; Germany ; History, 20th Century ; History, 21st Century ; Mitochondria/metabolism
    Language English
    Publishing date 2020-05-07
    Publishing country Germany
    Document type Biography ; Editorial ; Festschrift ; Historical Article ; Portrait
    ZDB-ID 1334659-3
    ISSN 1437-4315 ; 1431-6730 ; 1432-0355
    ISSN (online) 1437-4315
    ISSN 1431-6730 ; 1432-0355
    DOI 10.1515/hsz-2020-0151
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  9. Article ; Online: Shaping the mitochondrial inner membrane in health and disease.

    Colina-Tenorio, L / Horten, P / Pfanner, N / Rampelt, H

    Journal of internal medicine

    2020  Volume 287, Issue 6, Page(s) 645–664

    Abstract: Mitochondria play central roles in cellular energetics, metabolism and signalling. Efficient respiration, mitochondrial quality control, apoptosis and inheritance of mitochondrial DNA depend on the proper architecture of the mitochondrial membranes and a ...

    Abstract Mitochondria play central roles in cellular energetics, metabolism and signalling. Efficient respiration, mitochondrial quality control, apoptosis and inheritance of mitochondrial DNA depend on the proper architecture of the mitochondrial membranes and a dynamic remodelling of inner membrane cristae. Defects in mitochondrial architecture can result in severe human diseases affecting predominantly the nervous system and the heart. Inner membrane morphology is generated and maintained in particular by the mitochondrial contact site and cristae organizing system (MICOS), the F
    MeSH term(s) DNA, Mitochondrial/genetics ; Humans ; Mitochondria/genetics ; Mitochondria/metabolism ; Mitochondria/ultrastructure ; Mitochondrial Diseases/genetics ; Mitochondrial Diseases/metabolism ; Mitochondrial Membranes/metabolism ; Mitochondrial Membranes/ultrastructure ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Mitochondrial Proton-Translocating ATPases/genetics ; Mitochondrial Proton-Translocating ATPases/metabolism ; Mutation/genetics
    Chemical Substances DNA, Mitochondrial ; Mitochondrial Proteins ; Mitochondrial Proton-Translocating ATPases (EC 3.6.3.-)
    Language English
    Publishing date 2020-02-26
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 96274-0
    ISSN 1365-2796 ; 0954-6820
    ISSN (online) 1365-2796
    ISSN 0954-6820
    DOI 10.1111/joim.13031
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  10. Book ; Thesis: Zur Rolle des Membranpotentials beim Import mitochondrialer Vorstufenproteine

    Pfanner, Nikolaus

    1985  

    Author's details vorgelegt von Nikolaus Pfanner
    Size II, 48 S. : graph. Darst.
    Document type Book ; Thesis
    Thesis / German Habilitation thesis München, Univ., Diss., 1985
    HBZ-ID HT003262464
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
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