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Article ; Online: The multi-factor modulated biogenesis of the mitochondrial multi-span protein Om14.

Zhou, Jialin / Jung, Martin / Dimmer, Kai S / Rapaport, Doron

2022 Volume 221, Issue 4

Abstract: The mitochondrial outer membrane (MOM) harbors proteins that traverse the membrane via several helical segments and are called multi-span proteins. To obtain new insights into the biogenesis of these proteins, we utilized yeast mitochondria and the multi- ...

Abstract	The mitochondrial outer membrane (MOM) harbors proteins that traverse the membrane via several helical segments and are called multi-span proteins. To obtain new insights into the biogenesis of these proteins, we utilized yeast mitochondria and the multi-span protein Om14. Testing different truncation variants, we show that while only the full-length protein contains all the information that assures perfect targeting specificity, shorter variants are targeted to mitochondria with compromised fidelity. Employing a specific insertion assay and various deletion strains, we show that proteins exposed to the cytosol do not contribute significantly to the biogenesis process. We further demonstrate that Mim1 and Porin support optimal membrane integration of Om14 but none of them are absolutely required. Unfolding of newly synthesized Om14, its optimal hydrophobicity, and higher fluidity of the membrane enhanced the import capacity of Om14. Collectively, these findings suggest that MOM multi-span proteins follow different biogenesis pathways in which proteinaceous elements and membrane behavior contribute to a variable extent to the combined efficiency.
MeSH term(s)	Mitochondrial Membrane Transport Proteins/metabolism ; Mitochondrial Membranes/metabolism ; Protein Transport ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	MIM1 protein, S cerevisiae ; Mitochondrial Membrane Transport Proteins ; OM14 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins
Language	English
Publishing date	2022-03-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202112030
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Article ; Online: Hydrogenosomal tail-anchored proteins are targeted to both mitochondria and ER upon their expression in yeast cells.

Ferdigg, Andrè / Dimmer, Kai S / Rapaport, Doron / Vitali, Daniela G

PloS one

2020 Volume 15, Issue 8, Page(s) e0237982

Abstract: ... to the well-studied mitochondria import. Indeed, S. cerevisiae mitochondria and T. vaginalis hydrogenosomes ...

Abstract	Some organisms, like Trichomonas vaginalis, contain mitochondria-related hydrogen-producing organelles, called hydrogenosomes. The protein targeting into these organelles is proposed to be similar to the well-studied mitochondria import. Indeed, S. cerevisiae mitochondria and T. vaginalis hydrogenosomes share some components of protein import complexes. However, it is still unknown whether targeting signals directing substrate proteins to hydrogenosomes can support in other eukaryotes specific mitochondrial localization. To address this issue, we investigated the intracellular localization of three hydrogenosomal tail-anchored proteins expressed in yeast cells. We observed that these proteins were targeted to both mitochondria and ER with a variable dependency on the mitochondrial MIM complex. Our results suggest that the targeting signal of TA proteins are only partially conserved between hydrogenosomes and yeast mitochondria.
MeSH term(s)	Endoplasmic Reticulum/metabolism ; Gene Expression Regulation, Fungal ; Mitochondria/metabolism ; Protein Transport ; Saccharomyces cerevisiae/cytology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Trichomonas vaginalis/cytology ; Trichomonas vaginalis/genetics ; Trichomonas vaginalis/metabolism
Chemical Substances	Saccharomyces cerevisiae Proteins
Language	English
Publishing date	2020-08-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0237982
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Article ; Online: Interaction network of the mitochondrial outer membrane protein Mcp3.

Sinzel, Monika / Zeitler, Andreas / Dimmer, Kai S

FEBS letters

2018 Volume 592, Issue 19, Page(s) 3210–3220

Abstract: Mitochondria are organelles containing two membranes that are distinct in composition and function. A role of the mitochondrial outer membrane (MOM) is to mediate contact of the organelle with the rest of the cell. In yeast, the MOM contains about 40 ... ...

Abstract	Mitochondria are organelles containing two membranes that are distinct in composition and function. A role of the mitochondrial outer membrane (MOM) is to mediate contact of the organelle with the rest of the cell. In yeast, the MOM contains about 40 different integral proteins. Recently, we described the MOM protein Mcp3, which can serve as a multicopy suppressor of loss of ERMES complex that mediates mitochondria-endoplasmic reticulum contacts. To shed further light on the role of Mcp3 in the MOM, we analyzed its physical interaction with other proteins. We show that Mcp3 interacts with the MOM protein Om45 and the inner membrane protein Aim19. Our observations hint toward a potential involvement of Mcp3 in a structural and/or functional link between both mitochondrial membranes.
MeSH term(s)	Endoplasmic Reticulum/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mitochondria/metabolism ; Mitochondrial Membranes/metabolism ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Mutation ; Protein Binding ; Protein Interaction Maps ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	FUN14 protein, S cerevisiae ; MIC19 protein, S cerevisiae ; Membrane Proteins ; Mitochondrial Proteins ; Om45 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins
Language	English
Publishing date	2018-09-29
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1002/1873-3468.13243
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Article ; Online: Hydrogenosomal tail-anchored proteins are targeted to both mitochondria and ER upon their expression in yeast cells.

Andrè Ferdigg / Kai S Dimmer / Doron Rapaport / Daniela G Vitali

PLoS ONE, Vol 15, Iss 8, p e

2020 Volume 0237982

Abstract: ... to the well-studied mitochondria import. Indeed, S. cerevisiae mitochondria and T. vaginalis hydrogenosomes ...

Abstract	Some organisms, like Trichomonas vaginalis, contain mitochondria-related hydrogen-producing organelles, called hydrogenosomes. The protein targeting into these organelles is proposed to be similar to the well-studied mitochondria import. Indeed, S. cerevisiae mitochondria and T. vaginalis hydrogenosomes share some components of protein import complexes. However, it is still unknown whether targeting signals directing substrate proteins to hydrogenosomes can support in other eukaryotes specific mitochondrial localization. To address this issue, we investigated the intracellular localization of three hydrogenosomal tail-anchored proteins expressed in yeast cells. We observed that these proteins were targeted to both mitochondria and ER with a variable dependency on the mitochondrial MIM complex. Our results suggest that the targeting signal of TA proteins are only partially conserved between hydrogenosomes and yeast mitochondria.
Keywords	Medicine ; R ; Science ; Q
Subject code	570
Language	English
Publishing date	2020-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
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Article: Interaction network of the mitochondrial outer membrane protein Mcp3

Sinzel, Monika / Zeitler, Andreas / Dimmer, Kai S.

FEBS letters. 2018 Oct., v. 592, no. 19

2018

Abstract	Mitochondria are organelles containing two membranes that are distinct in composition and function. A role of the mitochondrial outer membrane (MOM) is to mediate contact of the organelle with the rest of the cell. In yeast, the MOM contains about 40 different integral proteins. Recently, we described the MOM protein Mcp3, which can serve as a multicopy suppressor of loss of ERMES complex that mediates mitochondria–endoplasmic reticulum contacts. To shed further light on the role of Mcp3 in the MOM, we analyzed its physical interaction with other proteins. We show that Mcp3 interacts with the MOM protein Om45 and the inner membrane protein Aim19. Our observations hint toward a potential involvement of Mcp3 in a structural and/or functional link between both mitochondrial membranes.
Keywords	mitochondria ; outer membrane proteins ; reticulum ; yeasts
Language	English
Dates of publication	2018-10
Size	p. 3210-3220.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	JOURNAL ARTICLE
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1002/1873-3468.13243
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Article ; Online: Independent evolution of functionally exchangeable mitochondrial outer membrane import complexes.

Vitali, Daniela G / Käser, Sandro / Kolb, Antonia / Dimmer, Kai S / Schneider, Andre / Rapaport, Doron

eLife

2018 Volume 7

Abstract: Assembly and/or insertion of a subset of mitochondrial outer membrane (MOM) proteins, including subunits of the main MOM translocase, require the fungi-specific Mim1/Mim2 complex. So far it was unclear which proteins accomplish this task in other ... ...

Abstract	Assembly and/or insertion of a subset of mitochondrial outer membrane (MOM) proteins, including subunits of the main MOM translocase, require the fungi-specific Mim1/Mim2 complex. So far it was unclear which proteins accomplish this task in other eukaryotes. Here, we show by reciprocal complementation that the MOM protein pATOM36 of trypanosomes is a functional analogue of yeast Mim1/Mim2 complex, even though these proteins show neither sequence nor topological similarity. Expression of pATOM36 rescues almost all growth, mitochondrial biogenesis, and morphology defects in yeast cells lacking Mim1 and/or Mim2. Conversely, co-expression of Mim1 and Mim2 restores the assembly and/or insertion defects of MOM proteins in trypanosomes ablated for pATOM36. Mim1/Mim2 and pATOM36 form native-like complexes when heterologously expressed, indicating that additional proteins are not part of these structures. Our findings indicate that Mim1/Mim2 and pATOM36 are the products of convergent evolution and arose only after the ancestors of fungi and trypanosomatids diverged.
MeSH term(s)	Biological Coevolution ; Gene Deletion ; Gene Expression Regulation, Fungal ; Genetic Complementation Test ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mitochondria/genetics ; Mitochondria/metabolism ; Mitochondrial Membrane Transport Proteins/genetics ; Mitochondrial Membrane Transport Proteins/metabolism ; Mitochondrial Membranes/metabolism ; Organelle Biogenesis ; Phosphorylation ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Protozoan Proteins/genetics ; Protozoan Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Trypanosoma brucei brucei/genetics ; Trypanosoma brucei brucei/metabolism
Chemical Substances	MIM1 protein, S cerevisiae ; Membrane Proteins ; Mitochondrial Membrane Transport Proteins ; Protein Isoforms ; Protozoan Proteins ; Saccharomyces cerevisiae Proteins
Language	English
Publishing date	2018-06-20
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.34488
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Article ; Online: The mitochondrial intermembrane space-facing proteins Mcp2 and Tgl2 are involved in yeast lipid metabolism.

Odendall, Fenja / Backes, Sandra / Tatsuta, Takashi / Weill, Uri / Schuldiner, Maya / Langer, Thomas / Herrmann, Johannes M / Rapaport, Doron / Dimmer, Kai Stefan

Molecular biology of the cell

2019 Volume 30, Issue 21, Page(s) 2681–2694

Abstract: Mitochondria are unique organelles harboring two distinct membranes, the mitochondrial inner and outer membrane (MIM and MOM, respectively). Mitochondria comprise only a subset of metabolic pathways for the synthesis of membrane lipids; therefore most ... ...

Abstract	Mitochondria are unique organelles harboring two distinct membranes, the mitochondrial inner and outer membrane (MIM and MOM, respectively). Mitochondria comprise only a subset of metabolic pathways for the synthesis of membrane lipids; therefore most lipid species and their precursors have to be imported from other cellular compartments. One such import process is mediated by the ER mitochondria encounter structure (ERMES) complex. Both mitochondrial membranes surround the hydrophilic intermembrane space (IMS). Therefore, additional systems are required that shuttle lipids between the MIM and MOM. Recently, we identified the IMS protein Mcp2 as a high-copy suppressor for cells that lack a functional ERMES complex. To understand better how mitochondria facilitate transport and biogenesis of lipids, we searched for genetic interactions of this suppressor. We found that
MeSH term(s)	Endoplasmic Reticulum/metabolism ; Epistasis, Genetic ; Lipase/genetics ; Lipase/metabolism ; Lipid Metabolism ; Mitochondrial Membrane Transport Proteins/genetics ; Mitochondrial Membrane Transport Proteins/metabolism ; Mitochondrial Membranes/metabolism ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Phosphatidylethanolamines/metabolism ; Protein Transport ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	MCP2 protein, S cerevisiae ; MIA40 protein, S cerevisiae ; Mitochondrial Membrane Transport Proteins ; Mitochondrial Proteins ; Phosphatidylethanolamines ; Saccharomyces cerevisiae Proteins ; phosphatidylethanolamine (39382-08-6) ; Lipase (EC 3.1.1.3) ; TGL3 protein, S cerevisiae (EC 3.1.1.3)
Language	English
Publishing date	2019-09-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E19-03-0166
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Article ; Online: Independent evolution of functionally exchangeable mitochondrial outer membrane import complexes

Daniela G Vitali / Sandro Käser / Antonia Kolb / Kai S Dimmer / Andre Schneider / Doron Rapaport

eLife, Vol

2018 Volume 7

Abstract	Assembly and/or insertion of a subset of mitochondrial outer membrane (MOM) proteins, including subunits of the main MOM translocase, require the fungi-specific Mim1/Mim2 complex. So far it was unclear which proteins accomplish this task in other eukaryotes. Here, we show by reciprocal complementation that the MOM protein pATOM36 of trypanosomes is a functional analogue of yeast Mim1/Mim2 complex, even though these proteins show neither sequence nor topological similarity. Expression of pATOM36 rescues almost all growth, mitochondrial biogenesis, and morphology defects in yeast cells lacking Mim1 and/or Mim2. Conversely, co-expression of Mim1 and Mim2 restores the assembly and/or insertion defects of MOM proteins in trypanosomes ablated for pATOM36. Mim1/Mim2 and pATOM36 form native-like complexes when heterologously expressed, indicating that additional proteins are not part of these structures. Our findings indicate that Mim1/Mim2 and pATOM36 are the products of convergent evolution and arose only after the ancestors of fungi and trypanosomatids diverged.
Keywords	mitochondria ; trypanosome ; outer membrane ; MIM complex ; biogenesis ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
Subject code	570
Language	English
Publishing date	2018-06-01T00:00:00Z
Publisher	eLife Sciences Publications Ltd
Document type	Article ; Online
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Article: (De)constructing mitochondria: what for?

Dimmer, Kai S / Scorrano, Luca

Physiology (Bethesda, Md.)

2006 Volume 21, Page(s) 233–241

Abstract: Mitochondria are dynamic organelles, essential for cell life and death. The morphology of this organelle is determined by fusion and fission, controlled by a growing set of "mitochondria-shaping" proteins, which influence crucial signalling cascades, ... ...

Abstract	Mitochondria are dynamic organelles, essential for cell life and death. The morphology of this organelle is determined by fusion and fission, controlled by a growing set of "mitochondria-shaping" proteins, which influence crucial signalling cascades, including apoptosis.
MeSH term(s)	Adenosine Triphosphate/metabolism ; Animals ; Apoptosis/physiology ; Cell Proliferation ; Cytoskeleton/physiology ; Cytoskeleton/ultrastructure ; DNA, Mitochondrial/genetics ; Dynamins ; GTP Phosphohydrolases/genetics ; GTP Phosphohydrolases/physiology ; Humans ; Mammals/physiology ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/physiology ; Mitochondria/physiology ; Mitochondria/ultrastructure ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/physiology ; Saccharomyces cerevisiae/physiology ; Saccharomyces cerevisiae/ultrastructure ; Signal Transduction/physiology
Chemical Substances	DNA, Mitochondrial ; Microtubule-Associated Proteins ; Mitochondrial Proteins ; Adenosine Triphosphate (8L70Q75FXE) ; GTP Phosphohydrolases (EC 3.6.1.-) ; OPA1 protein, human (EC 3.6.1.-) ; DNM1L protein, human (EC 3.6.5.5) ; Dynamins (EC 3.6.5.5)
Language	English
Publishing date	2006-07-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2158667-6
ISSN	1548-9221 ; 1548-9213
ISSN (online)	1548-9221
ISSN	1548-9213
DOI	10.1152/physiol.00010.2006
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Article ; Online: The cytosolic cochaperone Sti1 is relevant for mitochondrial biogenesis and morphology.

Hoseini, Hoda / Pandey, Saroj / Jores, Tobias / Schmitt, Anja / Franz-Wachtel, Mirita / Macek, Boris / Buchner, Johannes / Dimmer, Kai Stefan / Rapaport, Doron

The FEBS journal

2016 Volume 283, Issue 18, Page(s) 3338–3352

Abstract: Most mitochondrial proteins are synthesized in the cytosol prior to their import into the organelle. It is commonly accepted that cytosolic factors are required for delivering precursor proteins to the mitochondrial surface and for keeping newly ... ...

Abstract	Most mitochondrial proteins are synthesized in the cytosol prior to their import into the organelle. It is commonly accepted that cytosolic factors are required for delivering precursor proteins to the mitochondrial surface and for keeping newly synthesized proteins in an import-competent conformation. However, the identity of such factors and their defined contribution to the import process are mostly unknown. Using a presequence-containing model protein and a site-directed photo-crosslinking approach in yeast cells we identified the cytosolic chaperones Hsp70 (Ssa1) and Hsp90 (Hsp82) as well as their cochaperones, Sti1 and Ydj1, as putative cytosolic factors involved in mitochondrial protein import. Deletion of STI1 caused both alterations in mitochondrial morphology and lower steady-state levels of a subset of mitochondrial proteins. In addition, double deletion of STI1 with the mitochondrial import factors, MIM1 or TOM20, showed a synthetic growth phenotype indicating a genetic interaction of STI1 with these genes. Moreover, recombinant cytosolic domains of the import receptors Tom20 and Tom70 were able to bind in vitro Sti1 and other cytosolic factors. In summary, our observations point to a, direct or indirect, role of Sti1 for mitochondrial functionality.
MeSH term(s)	Adenosine Triphosphatases/metabolism ; Cross-Linking Reagents ; Cytosol/metabolism ; Gene Deletion ; Genes, Fungal ; HSP40 Heat-Shock Proteins/metabolism ; HSP70 Heat-Shock Proteins/metabolism ; HSP90 Heat-Shock Proteins/metabolism ; Heat-Shock Proteins/genetics ; Heat-Shock Proteins/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mitochondria/metabolism ; Mitochondria/ultrastructure ; Mitochondrial Membrane Transport Proteins/genetics ; Mitochondrial Membrane Transport Proteins/metabolism ; Mitochondrial Proteins/metabolism ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Organelle Biogenesis ; Protein Transport ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae/ultrastructure ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	Cross-Linking Reagents ; HSP40 Heat-Shock Proteins ; HSP70 Heat-Shock Proteins ; HSP82 protein, S cerevisiae ; HSP90 Heat-Shock Proteins ; Heat-Shock Proteins ; MIM1 protein, S cerevisiae ; Membrane Proteins ; Mitochondrial Membrane Transport Proteins ; Mitochondrial Proteins ; Molecular Chaperones ; Recombinant Proteins ; STI1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; TOM20 protein, S cerevisiae ; TOM70 protein, S cerevisiae ; YDJ1 protein, S cerevisiae (139874-78-5) ; Adenosine Triphosphatases (EC 3.6.1.-) ; SSA1 protein, S cerevisiae (EC 3.6.1.3)
Language	English
Publishing date	2016-09
Publishing country	England
Document type	Journal Article
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.13813
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