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1	RNA-binding proteins in yeast mitochondria / RNA-bindende Proteine in Hefemitochondrien Deumer, Claudia D. 06 December 2002 (has links) (PDF) This work focused on the further characterisation of Idhp and of the Krebs cycle enzymes citrate synthase 1 (Cit1p) and malate dehydrogenase 1 (Mdh1p) both of which have been identified as RNA-binding proteins without known RNA recognition motifs. Besides analysing their effects on mitochondrial translation and their organisation in protein complexes the work focused on the characterisation of the RNA-binding properties of recombinant Cit1p and Mdh1p: · Cit1p and Mdh1p play no essential role in mitochondrial protein synthesis. · Idhp is in a complex of molecular weight larger than the cytochrome c oxidase (250 kDa). · Cit1p and Mdh1p are in mitochondrial complexes smaller than 250 kDa. · 1000-fold molar excess of tRNA referring to COX2 leader RNA did not inhibit the RNA-binding of Cit1p and Mdh1p. · Cit1p and Mdh1p bind mitochondrial mRNAs (sense and antisense). The influence of cofactors and substrates on RNA-binding was analysed in order to reveal a possible link between the enzymatic function and the property of RNA-binding: · Acetyl-CoA and ATP inhibited the RNA-binding of Cit1p and Mdh1p at a concentration of 5 mM. Krebszyklusenzyme RNA-Bindung mitochondriale Translation Krebs cycle enzymes RNA-binding mitochondrial translation ddc:32 rvk:WG 1890 Citronensäurezyklus Enzym Hefeartige Pilze Mitochondrium RNS-Bindungsproteine Translation
2	RNA-binding proteins in yeast mitochondria Deumer, Claudia D. 09 October 2002 (has links) This work focused on the further characterisation of Idhp and of the Krebs cycle enzymes citrate synthase 1 (Cit1p) and malate dehydrogenase 1 (Mdh1p) both of which have been identified as RNA-binding proteins without known RNA recognition motifs. Besides analysing their effects on mitochondrial translation and their organisation in protein complexes the work focused on the characterisation of the RNA-binding properties of recombinant Cit1p and Mdh1p: · Cit1p and Mdh1p play no essential role in mitochondrial protein synthesis. · Idhp is in a complex of molecular weight larger than the cytochrome c oxidase (250 kDa). · Cit1p and Mdh1p are in mitochondrial complexes smaller than 250 kDa. · 1000-fold molar excess of tRNA referring to COX2 leader RNA did not inhibit the RNA-binding of Cit1p and Mdh1p. · Cit1p and Mdh1p bind mitochondrial mRNAs (sense and antisense). The influence of cofactors and substrates on RNA-binding was analysed in order to reveal a possible link between the enzymatic function and the property of RNA-binding: · Acetyl-CoA and ATP inhibited the RNA-binding of Cit1p and Mdh1p at a concentration of 5 mM. info:eu-repo/classification/ddc/32 ddc:32
3	Etablierung eines Nachweisverfahrens zur Untersuchung der räumlichen und zeitlichen Verteilung mitochondrial translatierter Proteine mit hochauflösender STED-Mikroskopie durch metabolische Markierung mit nicht-kanonischen Aminosäuren / Development of a protocol for the investigation of the spacial and temporal distribution of mitochondrially translated proteins with high resolution STED microscopy using metabolic labeling with non-canonical amino acids Heuser, Moritz Fabian 02 May 2017 (has links) No description available. 570 metabolische Markierung nicht-kanonische Aminosäuren mitochondriale Translation STED Proteinsynthese Mitochondrien CuAAC Click-Chemie metabolic labeling non canonical amino acids mitochondrial translation STED protein synthesis mitochondria CuAAC click chemistry Biologie (PPN619462639)

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RNA-binding proteins in yeast mitochondria / RNA-bindende Proteine in Hefemitochondrien

RNA-binding proteins in yeast mitochondria