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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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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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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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GCA2 is a Key Regulator of S-type Anion Channel, SLAC1

GCA2 is a Key Regulator of S-type Anion Channel, SLAC1

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2010全国植物生物学研讨会

作者： Yong-Fei Wang Arthur Korte Erwin Grill Julian I. Schroeder Division of Biological Sciences Cell and Developmental Biology Section University of California San Diego Institute of Plant Physiology & Ecology SIBS Chinese Academy of Sciences lehrstuhl für botanik Technische Universitt München

Stomatal pores,formed by two surrounding guard cells in the epidermis of plant leaves,allow gas exchange in leaves and control transpirational water loss to the *** aperture of stomatal pores is regulated by transport...

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GCA2 is a Key Regulator of S-type Anion Channel,SLAC1

GCA2 is a Key Regulator of S-type Anion Channel,SLAC1

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植物分子生物学与现代农业——2010全国植物生物学研讨...

作者： Arthur Korte Erwin Grill Julian I.Schroeder lehrstuhl für botanik Technische Universitt MünchenAm Hochanger 4D-85354 FreisingGermany Division of Biological Sciences Cell and Developmental Biology SectionUniversity of California San DiegoLa JollaCA 92093-0116USA.

Stomatal pores,formed by two surrounding guard cells in the epidermis of plant leaves, allow gas exchange in leaves and control transpirational water loss to the atmosphere. The aperture of stomatal pores is regulated by transport of osmotically active ions and metabolites,such as Cl- and malate,across guard cell *** reported recently that recessive mutations in the SLAC1gene result in insensitivity of Arabidopsis

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GCA2 is a Key Regulator of S-type Anion Channel,SLAC1

GCA2 is a Key Regulator of S-type Anion Channel,SLAC1

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第六届中国植物逆境生理学与分子生物学学术研讨会

＜正＞Stomatal pores,formed by two surrounding guard cells in the epidermis of plant leaves,allow gas exchange in leaves and control transpirational water loss to the *** aperture of stomatal pores is regulated by transport of osmotically active ions and metabolites,such as Cl-and malate,across guard cell *** reported recently that recessive mutations in the SLAC1gene result in insensitivity of Arabidopsis

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Mutants, Overexpressors, and Interactors of Arabidopsis Plastocyanin Isoforms： Revised Roles of Plastocyanin in Photosynthetic Electron Flow and Thylakoid Redox State

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Molecular Plant 2009年第2期2卷 236-248页

作者： Paolo Pesaresi Michael Scharfenberg Martin Weigel Irene Granlund Wolfgang R Schroder Giovanni Finazzi Fabrice Rappaport Simona Masiero Antonella Furini Peter Jahns Dario Leister Dipartimento di Produzione Vegetale Universita degli studi di Milano c/o Parco Tecnologico Padano Via Einstein Loc Cascina Codazza 1-26900 Lodi Italy lehrstuhl fur botanik Department Biologie I Ludwig-Maximilians-Universitat Munchen GroBhaderner Str. 2 D-82152 Planegg-Martinsried Germany Abteilung fhr Pflanzenzuchtung und Genetik Max-Planck-lnstitut fur Zhchtungsforschung Carl-von-Linne-Weg 10 D-50829 Koln Germany Institute of Chemistry and Umea Plant Science Centre (UPSC) Umea University SE-901 87 Umea Sweden Institut de Biologie Physico-Chimique UMR 7141 CNRS-Universite R et M. Curie 13 rue Pierre et Marie Curie F-75005 Paris France Dipatimento di Biologia Universita degli studi di Milano Via Celoria 26 L-20133 Milano Italy Dipartimento Scientifico e Tecnologico Universita degli studi di Verona Strade le Grazie 15 1-37134 Verona Italy Institut fur Biochemie der Pflanzen Heinrich-Heine-Universitat Dusseldorf Universitatsstr. 1 D-40225 Dusseldorf Germany

Two homologous plastocyanin isoforms are encoded by the genes PETE1 and PETE2 in the nuclear genome of Arabidopsis thaliana. The PETE2 transcript is expressed at considerably higher levels and the PETE2 protein is the more abundant isoform. Null mutations in the PETE genes resulted in plants, designated pete1 and pete2, with decreased plastocyanin contents. However, despite reducing plastocyanin levels by over -90%, a pete2 null mutation on its own affects rates of photosynthesis and growth only slightly, whereas pete1 knockout plants, with about 60-80% of the wild-type plastocyanin level, did not show any alteration. Hence, plastocyanin concentration is not limiting for photosynthetic elec- tron flow under optimal growth conditions, perhaps implying other possible physiological roles for the protein. Indeed, plastocyanin has been proposed previously to cooperate with cytochrome C6A （Cyt C6A） in thylakoid redox reactions, but we find no evidence for a physical interaction between the two proteins, using interaction assays in yeast. We observed homodimerization of Cyt C6A in yeast interaction assays, but also Cyt C6A homodimers failed to interact with plastocyanin. Moreover, phenotypic analysis of atc6-1 pete1 and atc6-1 pete2 double mutants, each lacking Cyt C6A and one of the two piastocyanin-encoding genes, failed to reveal any genetic interaction. Overexpression of either PETE1 or PETE2 in the pete1 pete2 double knockout mutant background results in essentially wild-type photosynthetic performance, excluding the possibility that the two plastocyanin isoforms could have distinct functions in thylakoid electron flow.

关键词： Mutants Overexpressors nteractors of Arabidopsis Plastocyanin Isoforms

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