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Chloroplast Proteins without Cleavable Transit Peptides： Rare Exceptions or a Major Constituent of the Chloroplast Proteome？

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Molecular Plant 2009年第6期2卷 1325-1335页

作者： Ute Armbruster Alexander Hertle Elina Makarenko Jessica Zuhlke Mathias Pribil Angela Dietzmann ivo Schliebner Elena Aseeva Elena Fenino Michael Scharfenberg Christian Voigt Dario Leister Lehrstuhl fur botanik Department Biologie I Ludwig-Maximilians-Universit~t MQnchen Menzinger Str. 67 D-80638 Munchen Germany

Most chloroplast proteins （cp proteins） are nucleus-encoded, synthesized on cytosolic ribosomes as precursor proteins containing a presequence （cTP）, and post-translationally imported via the Tic/Toc complex into the organelle, where the cTP is removed. Only a few unambiguous instances of cp proteins that do not require cTPs （non-canonical cp proteins） have been reported so far. However, the survey of data from large-scale proteomic studies presented here suggests that the fraction of such proteins in the total cp proteome might be as large as -30%. To explore this discrepancy, we chose a representative set of 28 putative non-canonical cp proteins, and used in vitro import and Red Fluorescent Protein （RFP）-fusion assays to determine their sub-cellular destinations. Four proteins, including embryo defective 1211, glycolate oxidase 2, protein disulfide isomerase-like protein （PDii）, and a putative glutathione S-transferase, could be unambiguously assigned to the chloroplast. Several others （＇potential cp proteins＇） were found to be imported into chloroplasts in vitro, but failed to localize to the organelle when RFP was fused to their C-terminal ends. Extrapolations suggest that the fraction of cp proteins that enter the inner compartments of the organelle, although they lack a cTP, might be as large as 11.4% of the total cp proteome. Our data also support the idea that cytosolic proteins that associate with the cp outer membrane might account for false positive cp proteins obtained in earlier studies.

关键词： Chloroplast biology mitochondria organelle biogenesis/function protein targeting.

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Ycf1/Tic214 is Not Essential for the Accumulation of Plastid Proteins

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Molecular Plant 2017年第1期10卷 219-221页

作者： Bettina Bölter Jürgen Soll Department biologie i-botanik Ludwig-Maximilians-Universität Großhadernerstraße 2-4 82152 Planegg-Martinsried Germany

Dear Editor,Protein import into chloroplasts is an essential process for plant survival. Numerous studies in recent years have revealed many facts about the components involved and mechanistic features, but have also turned up some controversies. Especially the composition and function of the Tic （translocon at the inner enve- lope of chloroplasts） complex（es） are vividly debated. Whereas the importance of one central Tic component,

关键词： Essential Accumulation Proteins

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Nucleus-Encoded Light-Harvesting Chlorophyll a/b Proteins are imported Normally into Chlorophyll b-Free Chloroplasts of Arabidopsis

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Molecular Plant 2013年第3期6卷 860-871页

作者： Sabine Nick Jorg Meurer Jurgen Soil Elisabeth Ankele dept biologie i-botanik Biozentrum LMU Munchen Grosshadernerstrasse 2-4 D-82152 Planegg-Martinsried Germany Munich Center for integrated Protein Science ClPSM Ludwig-Maximilians-Universitat Munchen Feodor-Lynen-Strasse 25 D-81377 Munich Germany

Chloroplast-located proteins which are encoded by the nuclear genome have to be imported from the cytosol into the organelle in a posttranslational manner. Among these nuclear-encoded chloroplast proteins are the light- harvesting chlorophyll a/b-binding proteins （LHCPs）. After translation in the cytosol, precursor proteins of LHCPs are imported via the TOC/TiC translocase, processed to their mature size to insert into thylakoid membranes where they recruit chlorophylls a and b to form pigment-protein complexes. The translocation of proteins is a highly regulated process which employs several regulators. To analyze whether CAO （chlorophyll a oxigenase） which converts chlorophyll a to chlorophyll b at the inner chloroplast membrane, is one of these regulators, we performed import reactions utilizing a homozygous loss-of-function mutant （cao-1）. We imported in vitro translated and 35S-labeled precursor proteins of light- harvesting proteins of photosystem ii LHCB1, LHCB4, and LHCB5 into chloroplasts isolated from cao-1 and show that import of precursor proteins and their processing to mature forms are not impaired in the mutant. Therefore, regulation of the import machinery cannot be responsible for the decreased steady-state levels of light-harvesting complex （LHC） proteins. Regulation does not take place at the transcriptional level either, because Lhcb mRNAs are not down-regulated. Additionally, reduced steady-state levels of LHCPs also do not occur due to posttranslational turnover of non-functional LHCPs in chloroplasts. Taken together, our data show that plants in the absence of CAO and therefore devoid of chlorophyll b are not influenced in their import behavior of LHC proteins.

关键词： chloroplast import LHCPs cao-1 protein complex assembly thylakoid membranes photosynthesis.

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The Arabidopsis Protein CGLD11 is Required for Chloroplast ATP Synthase Accumulation

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Molecular Plant 2016年第6期9卷 885-899页

作者： Sabine Grahl Bennet Reiter irene Luise Gugel Evgenia Vamvaka Chiara Gandini Peter Jahns Jurgen Soil Dario Leister Thilo Ruhle Lehrstuhl fur Biochemie und Physiologie der Pflanzen (botanik) Department Biologie I Ludwig-Maximilians-Universitat Munchen 82152 Planegg-MartinsriedGermany Lehrstuhl for Molekularbiologie der Pflanzen (botanik) Department Biologie I Ludwig-MaximHians-Universitat MQnchen 82152 Planegg-Martinsried Germany Plant Biochemistry Heinrich-Heine-University DLisseldorf Universittsstrasse 1 40225 Desseldorf Germany Munich Centre for integrated Protein Science CiPSM Ludwig-Maximilians Universitat Menchen Butenandtstr. 5 - 13 81377 Munich Germany These authors contributed equally to this article.

ATP synthases in chloroplasts （cpATPase） and mitochondria （mtATPase） are responsible for ATP production during photosynthesis and oxidative phosphorylation, respectively. Both enzymes consist of two multi- subunit complexes, the membrane-bound coupling factor O and the soluble coupling factor 1. During cpATPase biosynthesis, several accessory factors facilitate subunit production and orchestrate complex assembly. Here, we describe a new auxiliary protein in Arabidopsis thaliana, which is required for cpATPase accumulation. AtCGLD11 （CONSERVED iN THE GREEN LiNEAGE AND DiATOMS 11） is a protein without any known functional domain and shows dual localization to chloroplasts and mitochondria. Loss of AtCGLDll function results in reduced levels of cpATPase and impaired photosynthetic performance with lower rates of ATP synthesis. in yeast two-hybrid experiments, AtCGLD11 interacts with the 13 subunits of the cpATPase and mtATPase. Our results suggest that AtCGLD11 functions in F1 assembly during cpATPase biogenesis, while its role in mtATPase biosynthesis may not, or not yet, be essential.

关键词： chloroplast mitochondria photosynthesis dual targeting ATP synthase assembly

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Update on Chloroplast Research： New Tools, New Topics, and New Trends

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Molecular Plant 2011年第1期4卷 1-16页

作者： Ute Armbruster Paolo Pesaresi Mathias Pribil Alexander Hertle Dario Leister Lehrstuhl for Molekularbiologie der Pflanzen (botanik) Department Biologie I Ludwig-Maximilians-Universitat M6nchen Groβhaderner Str. D-82152 Planegg-Martinsried Germany b Dipartimento di Scienze Biomolecolari e Biotecnologie Universita degli studi di Milano 1-20133 Milano Italy

Chloroplasts, the green differentiation form of plastids, are the sites of photosynthesis and other important plant functions. Genetic and genomic technologies have greatly boosted the rate of discovery and functional character- ization of chloroplast proteins during the past decade. indeed, data obtained using high-throughput methodologies, in particular proteomics and transcriptomics, are now routinely used to assign functions to chloroplast proteins. Our knowl- edge of many chloroplast processes, notably photosynthesis and photorespiration, has reached such an advanced state that biotechnological approaches to crop improvement now seem feasible. Meanwhile, efforts to identify the entire com- plement of chloroplast proteins and their interactions are progressing rapidly, making the organelle a prime target for systems biology research in plants.

关键词： Chloroplast biology genetics genomics molecular biology proteomics transcriptome analysis

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The Plastid Envelope CHLOROPLAST MANGANESE TRANSPORTER1 is Essential for Manganese Homeostasis in Arabidopsis

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Molecular Plant 2018年第7期11卷 955-969页

作者： Marion Eisenhut Natalie Hoecker Sidsel Birkelund Schmidt Rubek Merina Basgaran Samantha Flachbart Peter Jahns Tabea Eser Stefan Geimer Seren Husted Andreas P.M. Weber Dario Leister Anja Schneider Biochemie der Pflanzen Cluster of Excellence on Plant Science (CEPLAS) Heinrich-Heine-University Di3sseldorf 40225 Desseldorf Germany Molekularbiologie der Pflanzen (botanik) Department Biologie I Ludwig-Maximilians-University Mernchen 82152 Martinsried Germany Department of Plant and Environmental Sciences and Copenhagen Plant Science Centre (CPSC) Faculty of Science University of Copenhagen 1871 Frederiksberg Denmark Zellbiologie/Elektronenmikroskopie NW i/B1 Universit&t Bayreuth 95447 Bayreuth Germany These authors contributed equally to this article.

The transition metal manganese （Mn） is indispensable for photoautotrophic growth since photosystem ii （PSii） employs an inorganic Mn4CaOs cluster for water splitting. Here, we show that the Arabidopsis membrane protein CHLOROPLAST MANGANESE TRANSPORTER1 （CMT1） is involved in chloroplast Mn homeostasis. CMT1 is the closest homolog of the previously characterized thylakoid Mn transporter PHOTOSYNTHESiS-AFFECTED MUTANT71 （PAM71）. in contrast to PAM71, CMT1 resides at the chloro- plast envelope and is ubiquitously expressed. Nonetheless, like PAM71, the expression of CMT1 can also alleviate the Mn-sensitive phenotype of yeast mutant qomrl. The cmtl mutant is severely suppressed in growth, chloroplast ultrastructure, and PSii activity owing to a decrease in the amounts of pigments and thylakoid membrane proteins. The importance of CMT1 for chloroplast Mn homeostasis is demonstratedby the significant reduction in chloroplast Mn concentrations in cmtl-1, which exhibited reduced Mn binding in PSii complexes. Moreover, CMT1 expression is downregulated in Mn-surplus conditions. The pam71 cmtl-ldouble mutant resembles the cmtl-f single mutant rather than pare71 in most respects. Taken together, our results suggest that CMT1 mediates Mn2 uptake into the chloroplast stroma, and that CMT1 and PAM71 function sequentially in Mn delivery to PSii across the chloroplast envelope and the thylakoid membrane.

关键词： manganese transporter envelope chloroplast photosynthesis Arabidopsis

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Alb4 of Arabidopsis Promotes Assembly and Stabilization of a Non Chlorophyll-Binding Photosynthetic Complex, the CF1CF0-ATP Synthase

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Molecular Plant 2009年第6期2卷 1410-1424页

作者： Monique Benz Thomas Bals irene Luise Gugel Markus Piotrowski Andreas Kuhn Danja Schunemann Jurgen Soll Elisabeth Ankele Department of biologie i-botanik Biozentrum Ludwig-Maximillians-University Munich Grosshadernerstrasse 2-4 D-82152 Planegg-Martinsried Germany Munich Centre for integrated Protein Science CiPSM Ludwig-Maximillians-University Munich Feodor-Lynen-Strasse 25 D-81377 Munich Germany Department of Plant Physiology Ruhr-University Bochum D-44780 Bochum Germany Department of Microbiology University of Hohenheim Garbenstrasse 30 D-70599 Hohenheim Germany

All members of the YidC/Oxal/Alb3 protein family are evolutionarily conserved and appear to function in membrane protein integration and protein complex stabilization. Here, we report on a second thylakoidal isoform of Alb3, named Alb4. Analysis of Arabidopsis knockout mutant lines shows that Aib4 is required in assembly and/or stability of the CF1CF0-ATP synthase （ATPase）. alb4 mutant lines not only have reduced steady-state levels of ATPase subunits, but also their assembly into high-molecular-mass complexes is altered, leading to a reduction of ATP synthesis in the mutants. Moreover, we show that Alb4 but not Aib3 physically interacts with the subunits CF1β and CF0ll. Summarizing, the data indicate that Aib4 functions to stabilize or promote assembly of CF1 during its attachment to the membrane-embedded CF0 part.

关键词： Alb4 Alb3 Arabidopsis thylakoid membrane protein insertion protein complex assembly CF1CF0-ATP synthase.

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Red Light-induced Phytochrome Relocation into the Nucleus in Adiantum capillus-veneris

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Molecular Plant 2012年第3期5卷 611-618页

作者： Hidenori Tsuboi Sachihiko Nakamura Eberhard Schaifer Masamitsu Wadaa Kyushu University Hakozaki 6-10-1 Fukuoka 812-8581 Japan Tokyo Metropolitan University Minami-Osawa 1-1 Hachioji Tokyo 192-0397 Japan biologie ii/institut f6r botanik University of Freiburg D-79104 Freiburg Germany Freiburg institute for Advanced Studies School of Life Sciences Freiburg Germany

Phytochromes in seed plants are known to move into nuclei in a red light-dependent manner with or without interacting factors. Here, we show phytochrome relocation to the nuclear region in phytochrome-dependent Adiantum capillus-veneris spore germination by partial spore-irradiation experiments. The nuclear or non-nuclear region of imbibed spores was irradiated with a microbeam of red and/or far-red light and the localization of phytochrome involved in spore germination was estimated from the germination rate. The phytochrome for spore germination existed throughout whole spore under darkness after imbibition, but gradually migrated to the nuclear region following red light irradiation. in- tracellular distribution of PHY-GUS fusion proteins expressed in germinated spores by particle bombardment showed the migration of Acphy2, but not Acphyl, into nucleus in a red light-dependent manner, suggesting that Acphy2 is the photoreceptor for fern spore germination.

关键词： Adiantum capillus-veneris far-red light microbeam phytochrome red light spore germination

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A LiM Domain Protein from Tobacco involved in Actin-Bundling and Histone Gene Transcription

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Molecular Plant 2013年第2期6卷 483-502页

作者： Danièle Moes Sabrina Gatti CEline Hoffmann Monika Dieterle Flora Moreau Katrin Neumann Marc Schumacher Marc Diederich Erwin Grill Wen-Hui Shen André Steinmetz Cldment Thomas Centre de Recherche Public-SantE 84 Val Fleuri L-1526 Luxembourg Luxembourg Laboratoire de biologie Moleculaire et Cellulaire du Cancer HSpital Kirchberg 9 rue Edward Steichen L-2540 Luxembourg Luxembourg Lehrstuhl for botanik Technische Universitat Munchen EmiI-Ramann-StraBe 4 D-85354 Freising Germany Jnstitut de biologie Moleculaire des Plantes du CNRS 12 rue du Général Zimmer F-67084 Strasbourg Ceédex France

The two LiM domain-containing proteins from plants （LiMs） typically exhibit a dual cytoplasmic-nuclear dis-tribution, suggesting that, in addition to their previously described roles in actin cytoskeleton organization, they partici-pate in nuclear processes. Using a south-western blot-based screen aimed at identifying factors that bind to plant histone gene promoters, we isolated a positive clone containing the tobacco LiM protein WLiM2 （NtWLiM2） cDNA. Using both green fluorescent protein （GFP） fusion-and immunology-based strategies, we provide clear evidence that NtWLiM2 local-izes to the actin cytoskeleton, the nucleus, and the nucleolus. interestingly, the disruption of the actin cytoskeleton by latrunculin B significantly increases NtWLiM2 nuclear fraction, pinpointing a possible novel cytoskeletal-nuclear crosstalk. Biochemical and electron microscopy experiments reveal the ability of NtWLiM2 to directly bind to actin filaments and to crosslink the latter into thick actin bundles. Electrophoretic mobility shift assays show that NtWLiM2 specifically binds to the conserved octameric cis-elements （Oct） of the Arabidopsis histone H4A748 gene promoter and that this binding largely relies on both LiM domains. importantly, reporter-based experiments conducted in Arabidopsis and tobacco proto-plasts confirm the ability of NtWLiM2 to bind to and activate the H4A748 gene promoter in live cells. Expression studies indicate the constitutive presence of NtWLiM2 mRNA and NtWLiM2 protein during tobacco BY-2 cell proliferation and cell cycle progression, suggesting a role of NtWLiM2 in the activation of basal histone gene expression. interestingly, both live cell and in vitro data support NtWLiM2 di/oligomerization. We propose that NtWLiM2 functions as an actin-stabilizing protein, which, upon cytoskeleton remodeling, shuttles to the nucleus in order to modify gene expression.

关键词： actin BY-2 cytoskeleton DNA-binding histone genes LiM Nicotiana tabacum promoter regulation trans-acting factors.

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A Short Amino-Terminal Part of Arabidopsis Phytochrome A induces Constitutive Photomorphogenic Response

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Molecular Plant 2012年第3期5卷 629-641页

作者： Andra＇s Viczia＇n E＇va Ada＇m iris Wolf Ja＇nos Bindics Stefan Kircher Marc Heijde Roman Ulm Eberhard Scha＇fer Ferenc Nagy institute of Plant Biology Biological Research Centre of the Hungarian Academy of Sciences Temesva＇ri krt. 62. H-6726 Szeged Hungary biologie ii/institut for botanik University of Freiburg Freiburg Dermany Department of Botany and Plant Biology University of Geneva Geneva Switzerland Centre for Biological Signalling Studies （BiOSS） University of Freiburg Freiburg Germany School of Biological Sciences University of Edinburgh Edinburgh UK

Phytochrome A （phyA） is the dominant photoreceptor of far-red light sensing in Arabidopsis thaliana, phyA accumulates at high levels in the cytoplasm of etiolated seedlings, and light-induced phyA signaling is mediated by a com- plex regulatory network. This includes light- and FHY1/FHL protein-dependent translocation of native phyA into the nucleus in vivo. it has also been shown that a short N-terminal fragment of phyA （PHYA406） is sufficient to phenocopy this highly regulated cellular process in vitro. To test the biological activity of this N-terminal fragment of phyA in planta, we produced transgenic phyA-201 plants expressing the PHYA406-YFP （YELLOW FLUORESCENT PROTEiN）-DD, PHYA406- YFP-DD-NLS （nuclear localization signal）, and PHYA406-YFP-DD-NES （nuclear export signal） fusion proteins. Here, we report that PHYA406-YFP-DD is imported into the nucleus and this process is partially light-dependent whereas PHYA406-YFP-DD-NLS and PHYA406-YFP-DD-NES display the expected constitutive localization patterns. Our results show that these truncated phyA proteins are light-stable, they trigger a constitutive photomorphogenic-like response when localized in the nuclei, and neither of them induces proper phyA signaling. We demonstrate that in vitro and in vivo PHYA406 Pfr and Pr bind COP1, a general repressor of photomorphogenesis, and co-localize with it in nuclear bodies. Thus, we conclude that, in planta, the truncated PHYA406 proteins inactivate COP1 in the nuclei in a light-independent fashion.

关键词： Arabidopsis cop phenotype phytochrome A COP1

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