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A B S T R A C T B O O K – A B S T R A C T S O F T A L K S Session 3/4. Photobiology, photosynthesis, photorespiration, algae and marine biology THYLAKOID MEMBRANE TETHERING OF FERREDOXIN-NADP + OXIDOREDUCTASE (FNR): REDOX-REGULATED INTERACTION WITH TIC62 Minna Lintala 1 , Philipp Benz 2,3,4 , Anna Stengel 2,3 , Jürgen Soll 2,3 , Bettina Bölter 2,3 , Paula Mulo 1 1 Molecular Plant Biology, Department of Biochemistry and Food Chemistry, University of Turku, Turku, Finland 2 Munich Center for Integrated Protein Science CiPSM, Ludwig-Maximilians-UniversitätMünchen, Munich, Germany 3 Department of Biology I, Botany, Ludwig-Maximilians-UniversitätMünchen, Planegg-Martinsried, Germany 4 Present address: Energy Biosciences Institute, University of California at Berkeley, Berkeley, USA E-mail: mikali@utu.fi Ferredoxin-NADP + oxidoreductase (FNR) has a well defined role in catalyzing the final step of linear photosynthetic electron transfer chain. By performing electron transfer from ferredoxin to NADP + , FNR is an important mediator of reducing power from membrane-bound light reactions to the stromal metabolic pathways. In Arabidopsis thaliana, two chloroplast-targeted FNR isoforms FNR1 and FNR2 can be found attached to the thylakoid and inner envelope membranes, as well as in the stroma. We have shown that Tic62 protein binds FNR to thylakoid membranes. Formation of the large Tic62-FNR complexes is mediated by light and stromal redox-state. As photosynthesis is not affected in Arabidopsis tic62 mutant plants, which lack most of the thylakoid associated FNR, and because most of the FNR is released from the thylakoids in light, we presume that the soluble pool of FNR is highly capable of performing photosynthetic activity. We conclude that Tic62 represents a major FNR interaction partner not only at the inner envelope membrane but also at the thylakoid membrane of Arabidopsis thaliana. We furthermore propose that correct allocation of FNR is used to efficiently regulate Fddependent electron partitioning in the chloroplast. 23 X X I V S P P S C O N G R E S S 2 0 1 1
A B S T R A C T B O O K – A B S T R A C T S O F T A L K S Session 3/4. Photobiology, photosynthesis, photorespiration, algae and marine biology THIOREDOXIN INTERACTIONS IN THE CHLOROPLAST LUMEN OF ARABIDOPSIS THALIANA Michael Hall, Wolfgang Schröder,Thomas Kieselbach Department of Chemistry, Umeå University and Umeå Plant Science Center, Umeå, Sweden E-mail: michael.hall@chem.umu.se Thioredoxins, originally discovered as a link between photosynthesis and chloroplast metabolism, are a family of small disulfide-reductaseproteins found in all organisms. Arabidopsis thaliana has at least 44 known genes coding for thioredoxins or thioredoxinlike proteins, out of which 21 are predicted or experimentally shown to be located in plastids. Within the thylakoid membrane, the focal point of oxygenic photosynthesis, lays the thylakoid lumen, a small sub-organelle compartment containing a distinct protein population. The proteome of the thylakoid lumen of Arabidopsis thaliana is comprised of approximately 80 proteins. While many of the proteins have unknown functions, a number of them are important enzymes regulating processes such as oxygen-evolution and the xanthophyll cycle. Although no thioredoxin has so far been identified in the thylakoid lumen, several observations strongly indicate the presence of a thiotransduction pathway in the lumen: an x-ray structure study of the luminal immunophilin FKBP13 by Gopalan et al. showed that this protein contained two disulfide bonds which could be reduced by E.coli thioredoxin and Marchand et al. found that the extrinsic Photosystem II proteins PsbO1 and PsbO2, and also the luminal pentapeptide protein TL17 could be reduced by thioredoxin h3. We have identified putative thioredoxin targets in the chloroplast lumen of Arabidopsis thaliana using three complementary proteomic methods, fluorescence two-dimensional gel-electrophoresis, two-dimensional gel-electrophoresis coupled with differential alkylation and Trx affinity chromatography. In total we have identified 19 Trx target proteins, thus covering more than 40% of the currently known lumenal chloroplast proteome. We also show that the redox state of thiols is decisive for degradation of the extrinsic PsbO1 and PsbO2 subunits of photosystem II. Our current work is focused on functional and structural characterization of target proteins of unknown function, including the PsbP-domain proteins and pentapeptide repeat proteins. 24 X X I V S P P S C O N G R E S S 2 0 1 1
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Sponsors onsors ors A B S T R A C T
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