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","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"]]