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3nce upon a Time- Chloroplast Protein Imporl Research from Infancy to Future Challenges

Molecular Plant 2016年第6期9卷 798-812页

作者： bettina bolter Jurgen Soill Department Biotogie I-Botanik Ludwig-Maximilians-Universitat GroBhaderner Stral3e 2-4 82152 Planegg-Martinsried Germany Munich Center for Integrated Protein Science CiPSM Ludwig-Maximilians-Universitat Feodor-Lynen-Strasse 25 81377 Munich Germany

Protein import into chloroplasts has been a focus of research for several decades. The first publications dealing with this fascinating topic appeared in the 1970s. From the initial realization that many plastid proteins are being encoded for in the nucleus and require transport into their target organelle to the identification of import components in the cytosol, chloroplast envelopes, and stroma, as well as elucidation of some mechanistic details, more fascinating aspects are still being unraveled. With this overview, we present a survey of the beginnings of chloroplast protein import research, the first steps on this winding road, and end with a glimpse into the future.

关键词： chloroplast protein import historical perspective Toc Tic evolution envelope membranes

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Preprotein Import into Chloroplasts via the Toc and Tic Complexes Is Regulated by Redox Signals in Pisum sativum

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Molecular Plant 2009年第6期2卷 1181-1197页

作者： Anna Stengel J. Philipp Benz Bob B. Buchanan Jurgen Soil bettina bolter Munich Center for Integrated Protein Science CiPS^M 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 Plant and Microbial Biology University of California 411 Koshland Hall Berkeley CA 94720 USA

The import of nuclear-encoded preproteins is necessary to maintain chloroplast function. The recognition and transfer of most precursor proteins across the chloroplast envelopes are facilitated by two membrane-inserted protein complexes, the translocons of the chloroplast outer and inner envelope （Toc and Tic complexes, respectively）. Several signals have been invoked to regulate the import of preproteins. In our study, we were interested in redox-based import regulation mediated by two signals： regulation based on thiols and on the metabolic NADP＋/NADPH ratio. We sought to identify the proteins participating in the regulation of these transport pathways and to characterize the preprotein subgroups whose import is redox-dependent. Our results provide evidence that the formation and reduction of disulfide bridges in the Toc receptors and Toc translocation channel have a strong influence on import yield of all tested preproteins that depend on the Toc complex for translocation. Furthermore, the metabolic NADP＋/NADPH ratio influences not only the composition of the Tic complex, but also the import efficiency of most, but not all, preproteins tested. Thus, several Tic subcomplexes appear to participate in the translocation of different preprotein subgroups, and the redox-active compo- nents of these complexes likely play a role in regulating transport.

关键词： Metabolic regulation molecular transport transport processes/kinetics chloroplast biology protein targeting.

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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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