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  • 1
    Language: English
    In: The Plant cell, 2015-01-01, Vol.27 (1), p.189-201
    Description: Phytochromes function as red/far-red photoreceptors in plants and are essential for light-regulated growth and development. Photomorphogenesis, the developmental program in light, is the default program in seed plants. In dark-grown seedlings, photomorphogenic growth is suppressed by the action of the CONSTITUTIVELY PHOTOMORPHOGENIC1 (COP1)/SUPPRESSOR OF (SPA) complex, which targets positive regulators of photomorphogenic growth for degradation by the proteasome. Phytochromes inhibit the COP1/SPA complex, leading to the accumulation of transcription factors promoting photomorphogenesis; yet, the mechanism by which they inactivate COP1/SPA is still unknown. Here, we show that lightactivated phytochrome A (phyA) and phytochrome B (phyB) interact with SPA1 and other SPA proteins. Fluorescence resonance energy transfer-fluorescence lifetime imaging microscopy analyses show that SPAs and phytochromes colocalize and interact in nuclear bodies. Furthermore, light-activated phyA and phyB disrupt the interaction between COP1 and SPAs, resulting in reorganization of the COP1/SPA complex in planta. The light-induced stabilization of HFR1, a photomorphogenic factor targeted for degradation by COP1/SPA, correlates temporally with the accumulation of phyA in the nucleus and localization of phyA to nuclear bodies. Overall, these data provide a molecular mechanism for the inactivation of the COP1/SPA complex by phyA- and phyB-mediated light perception.
    Subject(s): Proteins ; Yeasts ; Hypocotyls ; Microscopy ; RESEARCH ARTICLES ; Antibodies ; Fluorescence ; Plants ; Physiological regulation ; Seedlings ; Plant cells ; Arabidopsis Proteins - metabolism ; Phytochrome A - metabolism ; Phytochrome B - metabolism ; Gene Expression Regulation, Plant ; Fluorescence Resonance Energy Transfer ; Protein Binding ; Arabidopsis - metabolism ; Arabidopsis thaliana ; Chromophores ; Fluorescence microscopy ; Phytochrome
    ISSN: 1040-4651
    E-ISSN: 1532-298X
    Source: American Society of Plant Biologists
    Source: JSTOR Life Sciences
    Source: JSTOR Ecology & Botany II
    Source: Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
    Source: PubMed Central
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  • 2
    Language: English
    In: The Plant cell, 2006-03-01, Vol.18 (3), p.715-730
    Description: In eukaryotic cells, compartments of the highly dynamic endomembrane system are acidified to varying degrees by the activity of vacuolar H⁺-ATPases (V-ATPases). In the Arabidopsis thaliana genome, most V-ATPase subunits are encoded by small gene families, thus offering potential for a multitude of enzyme complexes with different kinetic properties and localizations. We have determined the subcellular localization of the three Arabidopsis isoforms of the membrane-integral V-ATPase subunit VHA-a. Colocalization experiments as well as immunogold labeling showed that VHA-a1 is preferentially found in the trans-Golgi network (TGN), the main sorting compartment of the secretory pathway. Uptake experiments with the endocytic tracer FM4-64 revealed rapid colocalization with VHA-a1, indicating that the TGN may act as an early endosomal compartment. Concanamycin A, a specific V-ATPase inhibitor, blocks the endocytic transport of FM4-64 to the tonoplast, causes the accumulation of FM4-64 together with newly synthesized plasma membrane proteins, and interferes with the formation of brefeldin A compartments. Furthermore, nascent cell plates are rapidly stained by FM4-64, indicating that endocytosed material is redirected into the secretory flow after reaching the TGN. Together, our results suggest the convergence of the early endocytic and secretory trafficking pathways in the TGN.
    Subject(s): Protein isoforms ; Proteins ; Tonoplast ; Yeasts ; Antibodies ; Cell membranes ; Plants ; Plant cells ; Seedlings ; Endosomes ; Isoenzymes - analysis ; Protein Subunits ; Pyridinium Compounds - analysis ; Arabidopsis - drug effects ; Arabidopsis - enzymology ; Intracellular Membranes - enzymology ; Plant Roots - metabolism ; Transport Vesicles - enzymology ; Arabidopsis - ultrastructure ; Vacuolar Proton-Translocating ATPases - metabolism ; Plant Roots - ultrastructure ; Endocytosis - physiology ; Plant Roots - drug effects ; trans-Golgi Network - drug effects ; Quaternary Ammonium Compounds - analysis ; Macrolides - pharmacology ; Biological Transport - physiology ; Vacuolar Proton-Translocating ATPases - analysis ; trans-Golgi Network - chemistry ; trans-Golgi Network - enzymology
    ISSN: 1040-4651
    E-ISSN: 1532-298X
    Source: American Society of Plant Biologists
    Source: JSTOR Life Sciences
    Source: JSTOR Ecology & Botany II
    Source: Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
    Source: PubMed Central
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  • 3
    Language: English
    In: Applied and Environmental Microbiology, 2014-02-01, Vol.80 (3), p.1051-1061
    Description: Classifications Services AEM Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue AEM About AEM Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy AEM RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0099-2240 Online ISSN: 1098-5336 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to AEM .asm.org, visit: AEM       
    Subject(s): Anaerobiosis ; Oxidation-Reduction ; Acetates - metabolism ; Betaproteobacteria - growth & development ; Betaproteobacteria - metabolism ; Comamonadaceae - growth & development ; Nitrites - metabolism ; Betaproteobacteria - ultrastructure ; Microscopy, Electron ; Nitrates - metabolism ; Periplasm - metabolism ; Ferrous Compounds - metabolism ; Denitrification ; Minerals - metabolism ; Comamonadaceae - ultrastructure ; Comamonadaceae - metabolism ; Physiological aspects ; Oxidation-reduction reaction ; Bacteria ; Iron ; Chemical properties ; Research ; Geomicrobiology
    ISSN: 0099-2240
    E-ISSN: 1098-5336
    Source: HighWire Press (Free Journals)
    Source: Hellenic Academic Libraries Link
    Source: PubMed Central
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  • 4
    Language: English
    In: The Plant cell, 2009-04-01, Vol.21 (4), p.1141-1154
    Description: Plant growth and organ formation depend on the oriented deposition of load-bearing cellulose microfibrils in the cell wall. Cellulose is synthesized by plasma membrane-bound complexes containing cellulose synthase proteins (CESAs). Here, we establish a role for the cytoskeleton in intracellular trafficking of cellulose synthase complexes (CSCs) through the in vivo study of the green fluorescent protein (GFP)-CESA3 fusion protein in Arabidopsis thaliana hypocotyls. GFP-CESA3 localizes to the plasma membrane, Golgl apparatus, a compartment identified by the VHA-a1 marker, and, surprisingly, a novel microtubule-associated cellulose synthase compartment (MASC) whose formation and movement depend on the dynamic cortical microtubule array. Osmotic stress or treatment with the cellulose synthesis inhibitor CGA 325'615 induces internalization of CSCs in MASCs, mimicking the intracellular distribution of CSCs in nongrowing cells. Our results indicate that cellulose synthesis is coordinated with growth status and regulated in part through CSC internalization. We find that CSC insertion in the plasma membrane is regulated by pauses of the Golgi apparatus along cortical microtubules. Our data support a model in which cortical microtubules not only guide the trajectories of CSCs in the plasma membrane, but also regulate the insertion and internalization of CSCs, thus allowing dynamic remodeling of CSC secretion during cell expansion and differentiation.
    Subject(s): Hypocotyls ; Cell walls ; Microtubules ; Epidermal cells ; Time series ; Cell membranes ; Trajectories ; Plants ; Plant cells ; Seedlings ; Arabidopsis - enzymology ; Glucosyltransferases - secretion ; Green Fluorescent Proteins - analysis ; Microtubules - physiology ; Recombinant Fusion Proteins - analysis ; Arabidopsis - ultrastructure ; Arabidopsis Proteins - secretion ; Golgi Apparatus - physiology ; Arabidopsis - metabolism ; Protein Transport ; Microtubules - metabolism ; Models, Biological ; Microtubules - ultrastructure ; Golgi Apparatus - ultrastructure ; Physiological aspects ; Genetic aspects ; Arabidopsis ; Growth ; Golgi apparatus ; Life Sciences ; Vegetal Biology
    ISSN: 1040-4651
    E-ISSN: 1532-298X
    Source: American Society of Plant Biologists
    Source: JSTOR Life Sciences
    Source: JSTOR Ecology & Botany II
    Source: Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
    Source: PubMed Central
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  • 5
    Language: English
    In: The Plant cell, 2010-04-01, Vol.22 (4), p.1344-1357
    Description: Plants constantly adjust their repertoire of plasma membrane proteins that mediates transduction of environmental and developmental signals as well as transport of ions, nutrients, and hormones. The importance of regulated secretory and endocytic trafficking is becoming increasingly clear; however, our knowledge of the compartments and molecular machinery involved is still fragmentary. We used immunogold electron microscopy and confocal laser scanning microscopy to trace the route of cargo molecules, including the BRASSINOSTEROID INSENSITIVE1 receptor and the REQUIRES HIGH BORON1 boron exporter, throughout the plant endomembrane system. Our results provide evidence that both endocytic and secretory cargo pass through the trans-Golgi network/early endosome (TGN/EE) and demonstrate that cargo in late endosomes/multivesicular bodies is destined for vacuolar degradation. Moreover, using spinning disc microscopy, we show that TGN/EEs move independently and are only transiently associated with an individual Golgi stack.
    Subject(s): Receptors ; Endocytosis ; Boron ; Cell walls ; Plants ; Freight ; Plant cells ; Endosomes ; Seedlings ; Golgi apparatus ; cell-wall pectins ; by-2 cells ; boron transporter ; root-cells ; homotypic fusion ; plant-cells ; prevacuolar compartments ; atpase activity ; endoplasmic-reticulum ; brefeldin-a ; Arabidopsis Proteins - metabolism ; Protein Kinases - metabolism ; Microscopy, Confocal ; Microscopy, Electron, Transmission ; trans-Golgi Network - metabolism ; Antiporters - metabolism ; Multivesicular Bodies - metabolism ; Arabidopsis - metabolism ; Protein Transport ; Arabidopsis thaliana ; Physiological aspects ; Research ; Plant physiology
    ISSN: 1040-4651
    E-ISSN: 1532-298X
    Source: American Society of Plant Biologists
    Source: JSTOR Life Sciences
    Source: JSTOR Ecology & Botany II
    Source: Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
    Source: PubMed Central
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  • 6
    Language: English
    In: The Journal of cell biology, 2007-10-22, Vol.179 (2), p.321-330
    Description: Primary cilia (PC) function as microtubule-based sensory antennae projecting from the surface of many eukaryotic cells. They play important roles in mechanoand chemosensory perception and their dysfunction is implicated in developmental disorders and severe diseases. The basal body that functions in PC assembly is derived from the mature centriole, a component of the centrosome. Through a small interfering RNA screen we found several centrosomal proteins (Ceps) to be involved in PC formation. One newly identified protein, Cep164, was indispensable for PC formation and hence characterized in detail. By immunogold electron microscopy, Cep164 could be localized to the distal appendages of mature centrioles. In contrast to ninein and Cep170, two components of subdistal appendages, Cep164 persisted at centrioles throughout mitosis. Moreover, the localizations of Cep164 and ninein/Cep170 were mutually independent during interphase. These data implicate distal appendages in PC formation and identify Cep164 as an excellent marker for these structures.
    Subject(s): Proteins ; 3T3 cells ; Centrosomes ; Cell cycle ; Antibodies ; Small interfering RNA ; HeLa cells ; Centrioles ; Appendages ; Cilia ; Carrier Proteins - ultrastructure ; Humans ; Cell Cycle Proteins - metabolism ; Cell Cycle Proteins - ultrastructure ; Protein Transport - drug effects ; Cilia - metabolism ; Antibodies - pharmacology ; Cell Nucleus Structures - drug effects ; Carrier Proteins - metabolism ; Cell Line, Tumor ; Cilia - drug effects ; Centrioles - metabolism ; Cell Cycle - drug effects ; Microtubule Proteins ; Centrioles - drug effects ; Cell Nucleus Structures - metabolism ; RNA, Small Interfering - metabolism ; s
    ISSN: 0021-9525
    E-ISSN: 1540-8140
    Source: HighWire Press (Free Journals)
    Source: Rockefeller University Press
    Source: Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
    Source: PubMed Central
    Source: Alma/SFX Local Collection
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  • 7
    Language: English
    In: The EMBO journal, 2011-06-01, Vol.30 (11), p.2246-2254
    Description: Conjugation is a major route of horizontal gene transfer, the driving force in the evolution of bacterial genomes. Antibiotic producing soil bacteria of the genus Streptomyces transfer DNA in a unique process involving a single plasmid‐encoded protein TraB and a double‐stranded DNA molecule. However, the molecular function of TraB in directing DNA transfer from a donor into a recipient cell is unknown. Here, we show that TraB constitutes a novel conjugation system that is clearly distinguished from DNA transfer by a type IV secretion system. We demonstrate that TraB specifically recognizes and binds to repeated 8 bp motifs on the conjugative plasmid. The specific DNA recognition is mediated by helix α3 of the C‐terminal winged‐helix‐turn‐helix domain of TraB. We show that TraB assembles to a hexameric ring structure with a central ∼3.1 nm channel and forms pores in lipid bilayers. Structure, sequence similarity and DNA binding characteristics of TraB indicate that TraB is derived from an FtsK‐like ancestor protein, suggesting that Streptomyces adapted the FtsK/SpoIIIE chromosome segregation system to transfer DNA between two distinct Streptomyces cells. Most bacteria share virulence and resistance genes by transferring single‐stranded DNA through a type IV secretion system. Streptomycetes, however, exchange dsDNA, using a system found to closely resemble machineries for prokaryotic chromosome segregation or DNA translocation during spore formation.
    Subject(s): TraB ; SpoIIIE ; conjugation ; conjugative DNA transfer ; FtsK ; Conjugation, Genetic ; Chromosome Segregation ; Chromosomes, Bacterial - genetics ; DNA, Bacterial - metabolism ; Streptomyces coelicolor - genetics ; Protein Multimerization ; Gene Transfer, Horizontal ; DNA - metabolism ; Phylogeny ; Sequence Analysis, DNA ; Sequence Homology, Amino Acid ; Plasmids ; Protein Binding ; Bacterial Proteins - metabolism ; Binding Sites ; Evolution, Molecular
    ISSN: 0261-4189
    E-ISSN: 1460-2075
    Source: HighWire Press (Free Journals)
    Source: PubMed Central
    Source: Alma/SFX Local Collection
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  • 8
    Language: English
    In: Microscopy research and technique, 2020-06, Vol.83 (6), p.691-705
    Description: For nearly 50 years immunogold labeling on ultrathin sections has been successfully used for protein localization in laboratories worldwide. In theory and in practice, this method has undergone continual improvement over time. In this study, we carefully analyzed circulating protocols for postembedding labeling to find out if they are still valid under modern laboratory conditions, and in addition, we tested unconventional protocols. For this, we investigated immunolabeling of Epon‐embedded cells, immunolabeling of cells treated with osmium, and the binding behavior of differently sized gold particles. Here we show that (in contrast to widespread belief) immunolabeling of Epon‐embedded cells and of cells treated with osmium tetroxide is actually working. Furthermore, we established a “speed protocol” for immunolabeling by reducing antibody incubation times. Finally, we present our results on three‐dimensional immunogold labeling. Immunogold labeling of Epon resin sections containing osmium tetroxide is possible and could be applied when structural details are relevant. Mostly, incubation times for immunogold labeling can be shortened without significant loss of efficiency. Three‐dimensional postembedding immunogold labeling was successfully applied on serial sections of a prokaryotic cell.
    Subject(s): (serial) immunogold labeling ; Diatoms ; Archaea ; Epon 812—osmium tetroxide ; Immunohistochemistry - methods ; Microalgae - ultrastructure ; Microtomy - methods ; Osmium Tetroxide - chemistry ; Histological Techniques ; Antibodies - chemistry ; Epoxy Compounds - chemistry ; Desulfurococcaceae - ultrastructure ; Microscopy, Immunoelectron - methods
    ISSN: 1059-910X
    E-ISSN: 1097-0029
    Source: Alma/SFX Local Collection
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  • 9
    Language: English
    In: eLife, 2014-04-08, Vol.3, p.e02131-e02131
    Description: Membrane trafficking is essential to fundamental processes in eukaryotic life, including cell growth and division. In plant cytokinesis, post-Golgi trafficking mediates a massive flow of vesicles that form the partitioning membrane but its regulation remains poorly understood. Here, we identify functionally redundant Arabidopsis ARF guanine-nucleotide exchange factors (ARF-GEFs) BIG1-BIG4 as regulators of post-Golgi trafficking, mediating late secretion from the trans-Golgi network but not recycling of endocytosed proteins to the plasma membrane, although the TGN also functions as an early endosome in plants. In contrast, BIG1-4 are absolutely required for trafficking of both endocytosed and newly synthesized proteins to the cell-division plane during cytokinesis, counteracting recycling to the plasma membrane. This change from recycling to secretory trafficking pathway mediated by ARF-GEFs confers specificity of cargo delivery to the division plane and might thus ensure that the partitioning membrane is completed on time in the absence of a cytokinesis-interphase checkpoint. DOI: http://dx.doi.org/10.7554/eLife.02131.001.
    Subject(s): Arabidopsis Proteins - metabolism ; Endocytosis ; Cell Division ; Golgi Apparatus - metabolism ; Arabidopsis Proteins - secretion ; Arabidopsis - metabolism ; Protein Transport ; Seeds ; Cytokinesis ; Guanine ; Golgi apparatus ; Proteins ; Microscopy ; Phylogenetics ; Membrane trafficking ; Physiology ; Software ; Flowers & plants ; Recycling ; Molecular biology ; Guanine nucleotide exchange factor ; Localization ; Plant Biology ; ARF-GEF ; secretion ; Arabidopsis ; cell division ; post-Golgi trafficking ; recycling ; gegulation of vesicle traffic ; Cell Biology
    ISSN: 2050-084X
    E-ISSN: 2050-084X
    Source: PubMed Central
    Source: DOAJ Directory of Open Access Journals - Not for CDI Discovery
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  • 10
    Language: English
    In: The Plant cell, 2009-12-01, Vol.21 (12), p.3984-4001
    Description: Plastid-targeted proteins pass through the cytosol as unfolded precursors. If proteins accumulate in the cytosol, they can form nonspecific aggregates that cause severe cellular damage. Here, we demonstrate that high levels of plastid precursors are degraded through the ubiquitin-proteasome system (UPS) in Arabidopsis thaliana cells. The cytosolic heat shock protein cognate 70-4 (Hsc70-4) and E3 ligase carboxy terminus of HscTO-interacting protein (CHIP) were highly induced in plastid protein import2 plants, which had a T-DNA insertion at Toc159 and showed an albino phenotype and a severe defect in protein import into chloroplasts. Hsc70-4 and CHIP together mediated plastid precursor degradation when import-defective chloroplast-targeted reporter proteins were transiently expressed in protoplasts. Hsc70-4 recognized specific sequence motifs in transit peptides and thereby led to precursor degradation through the UPS. CHIP, which interacted with Hsc70-4, functioned as an E3 ligase in the Hsc70-4-mediated protein degradation. The physiological role of Hsc70-4 was confirmed by analyzing Hsc70-4 RNA interfernce plants in an hsc70-1 mutant background. Plants with lower Hsc70 levels exhibited abnormal embryogenesis, resulting in defective seedlings that displayed high levels of reactive oxygen species and monoubiquitinated Lhcb4 precursors. We propose that Hsc70-4 and CHIP mediate plastid-destined precursor degradation to prevent cytosolic precursor accumulation and thereby play a critical role in embryogenesis.
    Subject(s): Proteins ; Protein isoforms ; Chloroplasts ; Gels ; Reverse transcriptase polymerase chain reaction ; Protoplasts ; Antibodies ; Protein precursors ; Plastids ; Plant cells ; Oligonucleotide Array Sequence Analysis ; Plants, Genetically Modified - genetics ; HSC70 Heat-Shock Proteins - metabolism ; Ubiquitin - metabolism ; Ubiquitin-Protein Ligases - metabolism ; Phylogeny ; RNA, Plant - genetics ; Chloroplasts - metabolism ; Protein Folding ; Arabidopsis - metabolism ; Protein Precursors - metabolism ; Arabidopsis - genetics ; Arabidopsis Proteins - metabolism ; DNA, Bacterial - genetics ; Plants, Genetically Modified - metabolism ; Mutagenesis, Insertional ; Protein Processing, Post-Translational ; Proteasome Endopeptidase Complex - metabolism ; Arabidopsis thaliana ; Ubiquitin ; Heat shock proteins ; Physiological aspects ; Plant embryology ; Research ; Properties
    ISSN: 1040-4651
    E-ISSN: 1532-298X
    Source: American Society of Plant Biologists
    Source: JSTOR Life Sciences
    Source: JSTOR Ecology & Botany II
    Source: Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
    Source: PubMed Central
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