Publications by authors named "Carina Knorpp"

Sugar metabolism is intricately connected with mitochondria through the conversion of sugars to ATP, and through the production of carbon skeletons that can be used in anabolic processes. Sugar molecules also take part in signalling cascades. In this study we investigated the impact of sucrose on the expression of the Arabidopsis thaliana Nucleoside Diphosphate Kinase gene family (NDPK, EC 2.

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Here, we present the characterization of a plant NDPK exhibiting nuclease activity. This is the first identification of a nuclease localised in the intermembrane space of plant mitochondria. The recombinant pea NDPK3 protein cleaves not only supercoiled plasmid DNA, but also highly structured RNA molecules such as tRNAs or the 3'UTR of the atp9 mRNA suggesting that the NDPK3 nuclease activity has a structural requirement.

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The FtsH proteases, also called AAA proteases, are membrane-bound ATP-dependent metalloproteases. The Arabidopsis genome contains a total of 12 FtsH-like genes. Two of them, AtFtsH4 and AtFtsH11, encode proteins with a high similarity to Yme1p, a subunit of the i-AAA complex in yeast mitochondria.

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Alloplasmic lines of Brassica napus with rearranged Arabidopsis thaliana mitochondrial DNA are male sterile and vegetatively altered compared with B. napus cv. Hanna.

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We report the first crystal structure of a plant (Pisum sativum L. cv Oregon sugarpod) mitochondrial nucleoside diphosphate kinase. Similar to other eukaryotic nucleoside diphosphate kinases, the plant enzyme is a hexamer; the six monomers in the asymmetric unit are arranged as trimers of dimers.

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This study shows that the plant mitochondrial nucleoside diphosphate kinase (mNDPK) localizes to both the intermembrane space and to the mitochondrial inner membrane. We show that mNDPK is very firmly attached to the membrane. Co-immunoprecipitation experiments identified the adenine nucleotide translocator as an interaction partner.

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Mitochondrial AAA metalloproteases play a fundamental role in mitochondrial biogenesis and function. They have been identified in yeast and animals but not yet in plants. This work describes the isolation and sequence analysis of the full-length cDNA from the pea (Pisum sativum) with significant homology to the yeast matrix AAA (m-AAA) protease.

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