Mick, David U.

[["dc.bibliographiccitation.firstpage","141"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","154"],["dc.bibliographiccitation.volume","191"],["dc.contributor.author","Mick, David U."],["dc.contributor.author","Vukotic, Milena"],["dc.contributor.author","Piechura, Heike"],["dc.contributor.author","Meyer, Helmut E."],["dc.contributor.author","Warscheid, Bettina"],["dc.contributor.author","Deckers, Markus"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:45:15Z"],["dc.date.available","2017-09-07T11:45:15Z"],["dc.date.issued","2010"],["dc.description.abstract","Regulation of eukaryotic cytochrome oxidase assembly occurs at the level of Cox1 translation, its central mitochondria-encoded subunit. Translation of COX1 messenger RNA is coupled to complex assembly in a negative feedback loop: the translational activator Mss51 is thought to be sequestered to assembly intermediates, rendering it incompetent to promote translation. In this study, we identify Coa3 (cytochrome oxidase assembly factor 3; Yjl062w-A), a novel regulator of mitochondrial COX1 translation and cytochrome oxidase assembly. We show that Coa3 and Cox14 form assembly intermediates with newly synthesized Cox1 and are required for Mss51 association with these complexes. Mss51 exists in equilibrium between a latent, translational resting, and a committed, translation-effective, state that are represented as distinct complexes. Coa3 and Cox14 promote formation of the latent state and thus down-regulate COX1 expression. Consequently, lack of Coa3 or Cox14 function traps Mss51 in the committed state and promotes Cox1 synthesis. Our data indicate that Coa1 binding to sequestered Mss51 in complex with Cox14, Coa3, and Cox1 is essential for full inactivation."],["dc.identifier.doi","10.1083/jcb.201007026"],["dc.identifier.gro","3142844"],["dc.identifier.isi","000282648500014"],["dc.identifier.pmid","20876281"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6311"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/293"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Rockefeller Univ Press"],["dc.relation.issn","0021-9525"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Coa3 and Cox14 are essential for negative feedback regulation of COX1 translation in mitochondria"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1457"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Traffic"],["dc.bibliographiccitation.lastpage","1466"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Lupo, Domenico"],["dc.contributor.author","Vollmer, Christine"],["dc.contributor.author","Deckers, Markus"],["dc.contributor.author","Mick, David U."],["dc.contributor.author","Tews, Ivo"],["dc.contributor.author","Sinning, Irmgard"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:43:24Z"],["dc.date.available","2017-09-07T11:43:24Z"],["dc.date.issued","2011"],["dc.description.abstract","Mitochondrial ribosomes synthesize core subunits of the inner membrane respiratory chain complexes. In mitochondria, translation is regulated by mRNA-specific activator proteins and occurs on membrane-associated ribosomes. Mdm38/Letm1 is a conserved membrane receptor for mitochondrial ribosomes and specifically involved in respiratory chain biogenesis. In addition, Mdm38 and its higher eukaryotic homolog Letm1, function as K+/H+ or Ca2+/H+ antiporters in the inner membrane. Here, we identify the conserved ribosome-binding domain (RBD) of Mdm38 and determine the crystal structure at 2.1 angstrom resolution. Surprisingly, Mdm38(RBD) displays a 14-3-3-like fold despite any similarity to 14-3-3-proteins at the primary sequence level and thus represents the first 14-3-3-like protein in mitochondria. The 14-3-3-like domain is critical for respiratory chain assembly through regulation of Cox1 and Cytb translation. We show that this function can be spatially separated from the ion transport activity of the membrane integrated portion of Mdm38. On the basis of the phenotypes observed for mdm38 Delta as compared to Mdm38 lacking the RBD, we suggest a model that combining ion transport and translational regulation into one molecule allows for direct coupling of ion flux across the inner membrane, and serves as a signal for the translation of mitochondrial membrane proteins via its direct association with the protein synthesis machinery."],["dc.identifier.doi","10.1111/j.1600-0854.2011.01239.x"],["dc.identifier.gro","3142664"],["dc.identifier.isi","000295052500017"],["dc.identifier.pmid","21718401"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/93"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: DFG [FOR967]; Max-Planck Society"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1600-0854"],["dc.relation.issn","1398-9219"],["dc.title","Mdm38 is a 14-3-3-Like Receptor and Associates with the Protein Synthesis Machinery at the Inner Mitochondrial Membrane"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1570"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.lastpage","1580"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Bareth, Bettina"],["dc.contributor.author","Nikolov, Miroslav"],["dc.contributor.author","Lorenzi, Isotta"],["dc.contributor.author","Hildenbeutel, Markus"],["dc.contributor.author","Mick, David U."],["dc.contributor.author","Helbig, Christin"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Ott, Martin"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.editor","Fox, Thomas D."],["dc.date.accessioned","2020-12-10T18:16:05Z"],["dc.date.available","2020-12-10T18:16:05Z"],["dc.date.issued","2016"],["dc.description.abstract","The mitochondrial cytochrome c oxidase assembles in the inner membrane from subunits of dual genetic origin. The assembly process of the enzyme is initiated by membrane insertion of the mitochondria-encoded Cox1 subunit. During complex maturation, transient assembly intermediates, consisting of structural subunits and specialized chaperone-like assembly factors, are formed. In addition, cofactors such as heme and copper have to be inserted into the nascent complex. To regulate the assembly process, the availability of Cox1 is under control of a regulatory feedback cycle in which translation of COX1 mRNA is stalled when assembly intermediates of Cox1 accumulate through inactivation of the translational activator Mss51. Here we isolate a cytochrome c oxidase assembly intermediate in preparatory scale from coa1 Delta. mutant cells, using Mss51 as bait. We demonstrate that at this stage of assembly, the complex has not yet incorporated the heme a cofactors. Using quantitative mass spectrometry, we define the protein composition of the assembly intermediate and unexpectedly identify the putative methyltransferase Oms1 as a constituent. Our analyses show that Oms1 participates in cytochrome c oxidase assembly by stabilizing newly synthesized Cox1."],["dc.identifier.doi","10.1091/mbc.E15-12-0811"],["dc.identifier.eissn","1939-4586"],["dc.identifier.gro","3141687"],["dc.identifier.isi","000376456800004"],["dc.identifier.issn","1059-1524"],["dc.identifier.pmid","27030670"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75047"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1939-4586"],["dc.relation.issn","1059-1524"],["dc.title","Oms1 associates with cytochrome c oxidase assembly intermediates to stabilize newly synthesized Cox1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4128"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","4137"],["dc.bibliographiccitation.volume","33"],["dc.contributor.author","Bareth, Bettina"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Mick, David U."],["dc.contributor.author","Nikolov, Miroslav"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:47:07Z"],["dc.date.available","2017-09-07T11:47:07Z"],["dc.date.issued","2013"],["dc.description.abstract","Cox1, the core subunit of the cytochrome c oxidase, receives two heme a cofactors during assembly of the 13-subunit enzyme complex. However, at which step of the assembly process and how heme is inserted into Cox1 have remained an enigma. Shy1, the yeast SURF1 homolog, has been implicated in heme transfer to Cox1, whereas the heme a synthase, Cox15, catalyzes the final step of heme a synthesis. Here we performed a comprehensive analysis of cytochrome c oxidase assembly intermediates containing Shy1. Our analyses suggest that Cox15 displays a role in cytochrome c oxidase assembly, which is independent of its functions as the heme a synthase. Cox15 forms protein complexes with Shy1 and also associates with Cox1-containing complexes independently of Shy1 function. These findings indicate that Shy1 does not serve as a mobile heme carrier between the heme a synthase and maturing Cox1 but rather cooperates with Cox15 for heme transfer and insertion in early assembly intermediates of cytochrome c oxidase."],["dc.identifier.doi","10.1128/MCB.00747-13"],["dc.identifier.gro","3142276"],["dc.identifier.isi","000324912000015"],["dc.identifier.pmid","23979592"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6487"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1098-5549"],["dc.relation.issn","0270-7306"],["dc.title","The Heme a Synthase Cox15 Associates with Cytochrome c Oxidase Assembly Intermediates during Cox1 Maturation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","14"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Reviews Molecular Cell Biology"],["dc.bibliographiccitation.lastpage","20"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Mick, David U."],["dc.contributor.author","Fox, Thomas D."],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:45:06Z"],["dc.date.available","2017-09-07T11:45:06Z"],["dc.date.issued","2011"],["dc.description.abstract","Mitochondria maintain genome and translation machinery to synthesize a small subset of subunits of the oxidative phosphorylation system. To build up functional enzymes, these organellar gene products must assemble with imported subunits that are encoded in the nucleus. New findings on the early steps of cytochrome c oxidase assembly reveal how the mitochondrial translation of its core component, cytochrome c oxidase subunit 1 (Cox1), is directly coupled to the assembly of this respiratory complex."],["dc.identifier.doi","10.1038/nrm3029"],["dc.identifier.gro","3142810"],["dc.identifier.isi","000285544000010"],["dc.identifier.pmid","21179059"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/255"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: NIGMS NIH HHS [R01 GM029362-29, R01 GM029362]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1471-0072"],["dc.title","Inventory control: cytochrome c oxidase assembly regulates mitochondrial translation"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5202"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.lastpage","5214"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Brandner, Katrin"],["dc.contributor.author","Mick, David U."],["dc.contributor.author","Frazier, Ann E."],["dc.contributor.author","Taylor, Rebecca D."],["dc.contributor.author","Meisinger, Chris"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:54:12Z"],["dc.date.available","2017-09-07T11:54:12Z"],["dc.date.issued","2005"],["dc.description.abstract","The Saccharomyces cerevisiae Taz1 protein is the orthologue of human Tafazzin, a protein that when inactive causes Barth Syndrome (BTHS), a severe inherited X-linked disease. Taz1 is a mitochondrial acyltransferase involved in the remodeling of cardiolipin. We show that Taz1 is an outer mitochondrial membrane protein exposed to the intermembrane space (IMS). Transport of Taz1 into mitochondria depends on the receptor Tom5 of the translocase of the outer membrane (TOM complex) and the small Tim proteins of the IMS, but is independent of the sorting and assembly complex (SAM). TAZ1 deletion in yeast leads to growth defects on nonfermentable carbon sources, indicative of a defect in respiration. Because cardiolipin has been proposed to stabilize supercomplexes of the respiratory chain complexes III and IV, we assess supercomplexes in taz1 Delta mitochondria and show that these are destabilized in taz1 Delta mitochondria. This leads to a selective release of a complex IV monomer from the III,IV, supercomplex. In addition, assembly analyses of newly imported subunits into complex IV show that incorporation of the complex IV monomer into supercomplexes is affected in taz1 Delta mitochondria. We conclude that inactivation of Taz1 affects both assembly and stability of respiratory chain complexes in the inner membrane of mitochondria."],["dc.identifier.doi","10.1091/mbc.E05-03-0256"],["dc.identifier.gro","3143793"],["dc.identifier.isi","000233025000015"],["dc.identifier.pmid","16135531"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1347"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1059-1524"],["dc.title","Taz1, an outer mitochondrial membrane protein, affects stability and assembly of inner membrane protein complexes: Implications for Barth syndrome"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2379"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Human Molecular Genetics"],["dc.bibliographiccitation.lastpage","2393"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Reinhold, Robert"],["dc.contributor.author","Bareth, Bettina"],["dc.contributor.author","Balleininger, Martina"],["dc.contributor.author","Wissel, Mirjam"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Mick, David U."],["dc.date.accessioned","2017-09-07T11:44:14Z"],["dc.date.available","2017-09-07T11:44:14Z"],["dc.date.issued","2011"],["dc.description.abstract","Defects in mitochondrial energy metabolism lead to severe human disorders, mainly affecting tissues especially dependent on oxidative phosphorylation, such as muscle and brain. Leigh Syndrome describes a severe encephalomyopathy in infancy, frequently caused by mutations in SURF1. SURF1, termed Shy1 in Saccharomyces cerevisiae, is a conserved assembly factor for the terminal enzyme of the respiratory chain, cytochrome c oxidase. Although the molecular function of SURF1/Shy1 is still enigmatic, loss of function leads to cytochrome c oxidase deficiency and reduced expression of the central subunit Cox1 in yeast. Here, we provide insights into the molecular mechanisms leading to disease through missense mutations in codons of the most conserved amino acids in SURF1. Mutations affecting G(124) do not compromise import of the SURF1 precursor protein but lead to fast turnover of the mature protein within the mitochondria. Interestingly, an (YD)-D-274 exchange neither affects stability nor localization of the protein. Instead, SURF1(Y274D) accumulates in a 200 kDa cytochrome c oxidase assembly intermediate. Using yeast as a model, we demonstrate that the corresponding Shy1(Y344D) is able to overcome the stage where cytochrome c oxidase assembly links to the feedback regulation of mitochondrial Cox1 expression. However, Shy1(Y344D) impairs the assembly at later steps, most apparent at low temperature and exhibits a dominant-negative phenotype upon overexpression. Thus, exchanging the conserved tyrosine (Y-344) with aspartate in yeast uncouples translational regulation of Cox1 from cytochrome c oxidase assembly and provides evidence for the dual functionality of Shy1."],["dc.identifier.doi","10.1093/hmg/ddr145"],["dc.identifier.gro","3142715"],["dc.identifier.isi","000290849200008"],["dc.identifier.pmid","21470975"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/150"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1460-2083"],["dc.relation.issn","0964-6906"],["dc.title","Mimicking a SURF1 allele reveals uncoupling of cytochrome c oxidase assembly from translational regulation in yeast"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4347"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","4358"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Mick, David U."],["dc.contributor.author","Wagner, Karina"],["dc.contributor.author","van der Laan, Martin"],["dc.contributor.author","Frazier, Ann E."],["dc.contributor.author","Perschil, Inge"],["dc.contributor.author","Pawlas, Magdalena"],["dc.contributor.author","Meyer, Helmut E."],["dc.contributor.author","Warscheid, Bettina"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:49:24Z"],["dc.date.available","2017-09-07T11:49:24Z"],["dc.date.issued","2007"],["dc.description.abstract","Cytochrome c oxidase ( complex IV) of the respiratory chain is assembled from nuclear and mitochondrially-encoded subunits. Defects in the assembly process lead to severe human disorders such as Leigh syndrome. Shy1 is an assembly factor for complex IV in Saccharomyces cerevisiae and mutations of its human homolog, SURF1, are the most frequent cause for Leigh syndrome. We report that Shy1 promotes complex IV biogenesis through association with different protein modules; Shy1 interacts with Mss51 and Cox14, translational regulators of Cox1. Additionally, Shy1 associates with the subcomplexes of complex IV that are potential assembly intermediates. Formation of these subcomplexes depends on Coal (YIL157c), a novel assembly factor that cooperates with Shy1. Moreover, partially assembled forms of complex IV bound to Shy1 and Cox14 can associate with the bc1 complex to form transitional supercomplexes. We suggest that Shy1 links Cox1 translational regulation to complex IV assembly and supercomplex formation."],["dc.identifier.doi","10.1038/sj.emboj.7601862"],["dc.identifier.gro","3143423"],["dc.identifier.isi","000250467100006"],["dc.identifier.pmid","17882259"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/936"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley-blackwell"],["dc.relation.eissn","1460-2075"],["dc.relation.issn","0261-4189"],["dc.title","Shy1 couples Cox1 translational regulation to cytochrome c oxidase assembly"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","52"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],["dc.bibliographiccitation.lastpage","59"],["dc.bibliographiccitation.volume","1793"],["dc.contributor.author","Wagner, Karina"],["dc.contributor.author","Mick, David U."],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:47:34Z"],["dc.date.available","2017-09-07T11:47:34Z"],["dc.date.issued","2009"],["dc.description.abstract","The mitochondrial inner membrane has a central function for the energy metabolism of the cell. The respiratory chain generates a proton gradient across the inner mitochondrial membrane which is used to, produce ATP by the F(1)F(o)-ATPase. To maintain the electrochemical gradient the inner membrane represents, an efficient permeability barrier for small molecules. Nevertheless, metabolites as well as polypeptide chains need to be transported across the inner membrane while the electrochemical gradient is retained. While specialized metabolite carrier proteins mediate the transport of small molecules, dedicated protein translocation machineries in the inner mitochondrial membrane (so called TIM complexes) transport precursor proteins across the inner membrane. Here we describe the organization of the TIM complexes and discuss the current models as to how they mediate the posttranslational import of proteins across and into the inner mitochondrial membrane. (C) 2008 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.bbamcr.2008.05.026"],["dc.identifier.gro","3143165"],["dc.identifier.isi","000262738300008"],["dc.identifier.pmid","18590776"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/649"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0167-4889"],["dc.title","Protein transport machineries for precursor translocation across the inner mitochondrial membrane"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1937"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.lastpage","1944"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Bauerschmitt, Heike"],["dc.contributor.author","Mick, David U."],["dc.contributor.author","Deckers, Markus"],["dc.contributor.author","Vollmer, Christine"],["dc.contributor.author","Funes, Soledad"],["dc.contributor.author","Kehrein, Kirsten"],["dc.contributor.author","Ott, Martin"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Herrmann, Johannes M."],["dc.date.accessioned","2017-09-07T11:46:00Z"],["dc.date.available","2017-09-07T11:46:00Z"],["dc.date.issued","2010"],["dc.description.abstract","Biogenesis of respiratory chain complexes depends on the expression of mitochondrial-encoded subunits. Their synthesis occurs on membrane-associated ribosomes and is probably coupled to their membrane insertion. Defects in expression of mitochondrial translation products are among the major causes of mitochondrial disorders. Mdm38 is related to Letm1, a protein affected in Wolf-Hirschhorn syndrome patients. Like Mba1 and Oxa1, Mdm38 is an inner membrane protein that interacts with ribosomes and is involved in respiratory chain biogenesis. We find that simultaneous loss of Mba1 and Mdm38 causes severe synthetic defects in the biogenesis of cytochrome reductase and cytochrome oxidase. These defects are not due to a compromised membrane binding of ribosomes but the consequence of a mis-regulation in the synthesis of Cox1 and cytochrome b. Cox1 expression is restored by replacing Cox1-specific regulatory regions in the mRNA. We conclude, that Mdm38 and Mba1 exhibit overlapping regulatory functions in translation of selected mitochondrial mRNAs."],["dc.identifier.doi","10.1091/mbc.E10-02-0101"],["dc.identifier.gro","3142905"],["dc.identifier.isi","000278681700003"],["dc.identifier.pmid","20427570"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7570"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/361"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Soc Cell Biology"],["dc.relation.issn","1059-1524"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Ribosome-binding Proteins Mdm38 and Mba1 Display Overlapping Functions for Regulation of Mitochondrial Translation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]