Life without complex I: proteome analyses of an Arabidopsis mutant lacking the mitochondrial NADH dehydrogenase complex

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dc.identifier.uri http://dx.doi.org/10.15488/510
dc.identifier.uri http://www.repo.uni-hannover.de/handle/123456789/534
dc.contributor.author Fromm, Steffanie
dc.contributor.author Senkler, Jennifer
dc.contributor.author Eubel, Holger
dc.contributor.author Peterhansel, Christoph
dc.contributor.author Braun, Hans-Peter
dc.date.accessioned 2016-09-06T07:57:59Z
dc.date.available 2016-09-06T07:57:59Z
dc.date.issued 2016
dc.identifier.citation Fromm, Steffanie; Senkler, Jennifer; Eubel, Holger; Peterhansel, Christoph; Braun, Hans-Peter: Life without complex I: proteome analyses of an Arabidopsis mutant lacking the mitochondrial NADH dehydrogenase complex. In: Journal of Experimental Botany 67 (2016), Nr. 10, S. 3079-3093. DOI: http://dx.doi.org/10.1093/jxb/erw165
dc.description.abstract The mitochondrial NADH dehydrogenase complex (complex I) is of particular importance for the respiratory chain in mitochondria. It is the major electron entry site for the mitochondrial electron transport chain (mETC) and therefore of great significance for mitochondrial ATP generation. We recently described an Arabidopsis thaliana double-mutant lacking the genes encoding the carbonic anhydrases CA1 and CA2, which both form part of a plant-specific 'carbonic anhydrase domain' of mitochondrial complex I. The mutant lacks complex I completely. Here we report extended analyses for systematically characterizing the proteome of the ca1ca2 mutant. Using various proteomic tools, we show that lack of complex I causes reorganization of the cellular respiration system. Reduced electron entry into the respiratory chain at the first segment of the mETC leads to induction of complexes II and IV as well as alternative oxidase. Increased electron entry at later segments of the mETC requires an increase in oxidation of organic substrates. This is reflected by higher abundance of proteins involved in glycolysis, the tricarboxylic acid cycle and branched-chain amino acid catabolism. Proteins involved in the light reaction of photosynthesis, the Calvin cycle, tetrapyrrole biosynthesis, and photorespiration are clearly reduced, contributing to the significant delay in growth and development of the double-mutant. Finally, enzymes involved in defense against reactive oxygen species and stress symptoms are much induced. These together with previously reported insights into the function of plant complex I, which were obtained by analysing other complex I mutants, are integrated in order to comprehensively describe 'life without complex I'. eng
dc.description.sponsorship DFG/1186/Br1829/10–2
dc.language.iso eng
dc.publisher Oxford : Oxford Univ. Press
dc.relation.ispartofseries Journal of Experimental Botany 67 (2016), Nr. 10
dc.rights CC BY 3.0
dc.rights.uri https://creativecommons.org/licenses/by/3.0/
dc.subject Arabidopsis thaliana eng
dc.subject carbonic anhydrase eng
dc.subject complex I eng
dc.subject mitochondrial metabolism eng
dc.subject photosynthesis eng
dc.subject proteomics eng
dc.subject respiratory chain eng
dc.subject.ddc 500 | Naturwissenschaften ger
dc.title Life without complex I: proteome analyses of an Arabidopsis mutant lacking the mitochondrial NADH dehydrogenase complex
dc.type article
dc.type Text
dc.relation.essn 1460-2431
dc.relation.issn 0022-0957
dc.relation.doi http://dx.doi.org/10.1093/jxb/erw165
dc.bibliographicCitation.issue 10
dc.bibliographicCitation.volume 67
dc.bibliographicCitation.firstPage 3079
dc.bibliographicCitation.lastPage 3093
dc.description.version publishedVersion
tib.accessRights frei zug�nglich


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