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Arabidopsis tic62 trol Mutant Lacking Thylakoid- Bound Ferredoxin-NADP＋ Oxidoreductase Shows Distinct Metabolic Phenotype

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Molecular Plant 2014年第1期7卷 45-57页

作者： Minna Lintala Natalie Schuck Ina Thormaihlen Andreas Jungfer Katrin L. Weber Andreas P.M. Weber peter geigenberger Juirgen Soil Bettina Bolter Paula Mulo Molecular Plant Biology Department of Biochemistry University of Turku FI-20014 Turku Finland Munich Center for Integrated Protein Science CiPSM Ludwig-Maximilians-Universitat Munchen Feodor-Lynen-Strasse 25 D-81377 Munich Germany Department of Biology I Botany Ludwig-Maximilians-Universitat Munchen Groβhaderner Strasse 2-4 D-82152 Planegg-Martinsried Germany Department of Biology I Plant Metabolism Group Ludwig-Maximilians-Universitat Munchen Groβhaderner Strasse 2-4 D-82152 Planegg-Martinsried Germany Institute for Plant Biochemistry Cluster of Excellence on Plant Sciences (CEPLAS) Universitatsstrasse 1 D-40225 Dusseldorf Germany

Ferredoxin-NADP＋ oxidoreductase （FNR）, functioning in the last step of the photosynthetic electron transfer chain, exists both as a soluble protein in the chloroplast stroma and tightly attached to chloroplast membranes. Surface plasmon resonance assays showed that the two FNR isoforms, LFNR1 and LFNR2, are bound to the thylakoid membrane via the C-terminal domains of Tic62 and TROL proteins in a pH-dependent manner. The tic62 trol double mutants contained a reduced level of FNR, exclusively found in the soluble stroma. Although the mutant plants showed no visual phenotype or defects in the function of photosystems under any conditions studied, a low ratio of NADPH/NADP~ was detected. Since the CO2 fixation capacity did not differ between the tic62 trol plants and wild-type, it seems that the plants are able to funnel reducing power to most crucial reactions to ensure survival and fitness of the plants. However, the activity of malate dehydrogenase was down-regulated in the mutant plants. Apparently, the plastid metabolism is able to cope with substantial changes in directing the electrons from the light reactions to stromal metabolism and thus only few differences are visible in steady-state metabolite pool sizes of the tic62 trol plants.

关键词： carbon assimilation ferredoxin-NADP+ oxidoreductase photosynthesis chloroplast stromal metabolism Tic62 TROL.

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Thioredoxins Play a Crucial Role in Dynamic Acclimation of Photosynthesis in Fluctuating Light

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Molecular Plant 2017年第1期10卷 168-182页

作者： Ina Thormahlen Arkadius Zupok Josephin Rescher Jochen Leger Stefan Weissenberger Julia Groysman Anne Orwat Gilles Chatel-lnnocenti Emmanuelle Issakidis-Bourguet Ute Armbruster peter geigenberger Department Biologie I Ludwig-Maximilians-Universitat MQnchen Grosshaderner StraSe 2-4 82152 Martinsried Germany Max-Planck-lnstitut fur Molekulare Pflanzenphysiologie Department 3 Am Muhlenberg 1 14476 Potsdam-Golm Germany Institute of Plant Sciences Paris Saclay (IPS2) UMR 9213/UMR1403 Universite Paris Sud CNRS INRA Universit~ d'Evry Universite Paris Diderot Sorbonne Paris Cite Batiment 630 91405 Orsay France

Sunlight represents the energy source for photosynthesis and plant growth. When growing in the field, plant photosynthesis has to manage strong fluctuations in light intensities. Regulation based on the thio- redoxin （Trx） system is believed to ensure light-responsive control of photosynthetic reactions in the chlo- roplast. However, direct evidence for a role of this system in regulating dynamic acclimation of photosyn- thesis in fluctuating conditions is largely lacking. In this report we show that the ferredoxin-dependent Trxs ml and m2 as well as the NADPH-dependent NTRC are both indispensable for photosynthetic acclimation in fluctuating light intensities. Arabidopsis mutants with combined deficiency in Trxs ml and m2 show wild- type growth and photosynthesis under constant light condition, while photosynthetic parameters are strongly modified in rapidly alternating high and low light. Two independent trxmlm2 mutants show lower photosynthetic efficiency in high light, but surprisingly significantly higher photosynthetic efficiency in low light. Our data suggest that a main target of Trx ml and m2 is the NADP-malate dehydrogenase involved in export of excess reductive power from the chloroplast. The decreased photosynthetic efficiency in the high-light peaks may thus be explained by a reduced capacity of the trxm lm2 mutants in the rapid light acti-vation of this enzyme. In the ntrc mutant, dynamic responses of non-photochemical quenching of excita- tion energy and plastoquinone reduction state both were strongly attenuated in fluctuating light intensities, leading to a massive decrease in PSII quantum efficiency and a specific decrease in plant growth under these conditions. This is likely due to the decreased ability of the ntrc mutant to control the stromal NADP（H） redox poise. Taken together, our results indicate that NTRC is indispensable in ensuring the full range of dynamic responses of photosynthesis to optimize photosynthesis and maintain growth in fluc

关键词： arabidopsis chloroplast light signalling NTRC redox regulation thioredoxin

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TOM9.2 Is a Calmodulin-Binding Protein Critical for TOM Complex Assembly but Not for Mitochondrial Protein Import in Arabidopsis thaliana

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Molecular Plant 2017年第4期10卷 575-589页

作者： Nargis Parvin Chris Carrie Isabelle Pabst Antonia Laber Debabrata Laha Melanie V. Paul peter geigenberger Ralf Heermann Kirsten Jung Ute C. Vothknecht Fatima Chigri Department Biology I Botany Ludwig-Maximilians-University Munich GroBhaderner Stra6e 2-4 82152 Martinsried Germany Department Biology 1 Microbiology Ludwig-Maximilians-University Munich Grobhaderner Strabe 2-4 82152 Martinsried Germany Department of Biology Center for Integrated Protein Science (Munich) Ludwig-Maximilians-University Munich 81377 Munich Germany Center for Plant Molecular Biology Plant Physiology University of Tuebingen Auf der Morgenstelle 32 72076 Tuebingen Germany present address: Plant Cell Biology IZMB University of Bonn Kirschallee 153115 Bonn Germany Present address: Center for Plant Molecular Biology Developmental Genetics University of Tubingen Auf der Morgenstelle 32 72076 Tubingen Germany

The translocon on the outer membrane of mitochondria （TOM） facilitates the import of nuclear-encoded proteins. The principal machinery of mitochondrial protein transport seems conserved in eukaryotes; however, divergence in the composition and structure of TOM components has been observed between mammals, yeast, and plants. TOM9, the plant homolog of yeast Tom22, is significantly smaller due to a truncation in the cytosolic receptor domain, and its precise function is not understood. Here we provide evidence showing that TOM9.2 from Arabidopsis thaliana is involved in the formation of mature TOM com- plex, most likely by influencing the assembly of the pore-forming subunit TOM40. Dexamethasone- induced RNAi gene silencing of TOM9.2 results in a severe reduction in the mature TOM complex, and the assembly of newly imported TOM40 into the complex is impaired. Nevertheless, mutant plants are fully viable and no obvious downstream effects of the loss of TOM complex, i.e., on mitochondrial import ca- pacity, were observed. Furthermore, we found that TOM9.2 can bind calmodulin （CAM） in vitro and that CaM impairs the assembly of TOM complex in the isolated wild-type mitochondria, suggesting a regula- tory role of TOM9.2 and a possible integration of TOM assembly into the cellular calcium signaling network.

关键词： protein import plant mitochondria TOM complex calmodulin calcium signaling

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Editorial

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Molecular Plant 2009年第2期2卷 369-369页

作者： Bob B. Buchanan Karl-Josef Dietz peter geigenberger Jean-Pierre Jacquot peter Schürmann

It is a pleasure, indeed, to be part of this Special Redox Biology Issue of Molecular Plant--a journal yet to celebrate its second birthday. The harvest of papers is rich indeed： 17 research articles and four reviews covering a range of topics that will be divided and published in two separate issues of Molecular Plant--the current （Vol. 2, No. 2） and subsequent （Vol. 2, No. 3） issues.

关键词： GLUTAREDOXIN PLASTOCYANIN

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