Search Results - (Author, Cooperation:G. I. McFadden)
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1B. A. Curtis ; G. Tanifuji ; F. Burki ; A. Gruber ; M. Irimia ; S. Maruyama ; M. C. Arias ; S. G. Ball ; G. H. Gile ; Y. Hirakawa ; J. F. Hopkins ; A. Kuo ; S. A. Rensing ; J. Schmutz ; A. Symeonidi ; M. Elias ; R. J. Eveleigh ; E. K. Herman ; M. J. Klute ; T. Nakayama ; M. Obornik ; A. Reyes-Prieto ; E. V. Armbrust ; S. J. Aves ; R. G. Beiko ; P. Coutinho ; J. B. Dacks ; D. G. Durnford ; N. M. Fast ; B. R. Green ; C. J. Grisdale ; F. Hempel ; B. Henrissat ; M. P. Hoppner ; K. Ishida ; E. Kim ; L. Koreny ; P. G. Kroth ; Y. Liu ; S. B. Malik ; U. G. Maier ; D. McRose ; T. Mock ; J. A. Neilson ; N. T. Onodera ; A. M. Poole ; E. J. Pritham ; T. A. Richards ; G. Rocap ; S. W. Roy ; C. Sarai ; S. Schaack ; S. Shirato ; C. H. Slamovits ; D. F. Spencer ; S. Suzuki ; A. Z. Worden ; S. Zauner ; K. Barry ; C. Bell ; A. K. Bharti ; J. A. Crow ; J. Grimwood ; R. Kramer ; E. Lindquist ; S. Lucas ; A. Salamov ; G. I. McFadden ; C. E. Lane ; P. J. Keeling ; M. W. Gray ; I. V. Grigoriev ; J. M. Archibald
Nature Publishing Group (NPG)
Published 2012Staff ViewPublication Date: 2012-12-04Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Algal Proteins/genetics/metabolism ; Alternative Splicing/genetics ; Cell Nucleus/*genetics ; Cercozoa/cytology/*genetics/metabolism ; Cryptophyta/cytology/*genetics/metabolism ; Cytosol/metabolism ; *Evolution, Molecular ; Gene Duplication/genetics ; Gene Transfer, Horizontal/genetics ; Genes, Essential/genetics ; Genome/*genetics ; Genome, Mitochondrial/genetics ; Genome, Plant/genetics ; Genome, Plastid/genetics ; Molecular Sequence Data ; *Mosaicism ; Phylogeny ; Protein Transport ; Proteome/genetics/metabolism ; Symbiosis/*genetics ; Transcriptome/geneticsPublished by: -
2C. D. Goodman ; J. E. Siregar ; V. Mollard ; J. Vega-Rodriguez ; D. Syafruddin ; H. Matsuoka ; M. Matsuzaki ; T. Toyama ; A. Sturm ; A. Cozijnsen ; M. Jacobs-Lorena ; K. Kita ; S. Marzuki ; G. I. McFadden
American Association for the Advancement of Science (AAAS)
Published 2016Staff ViewPublication Date: 2016-04-16Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Animals ; Anopheles/*parasitology ; Antimalarials/*pharmacology/therapeutic use ; Atovaquone/*pharmacology/therapeutic use ; Cell Line ; Cytochromes b/*genetics ; Drug Resistance/*genetics ; Genes, Mitochondrial/genetics ; Humans ; Life Cycle Stages/drug effects/genetics ; Malaria/drug therapy/*parasitology/transmission ; Male ; Mice ; Mitochondria/*genetics ; Mutation ; Plasmodium berghei/*drug effects/genetics/growth & development ; Selection, GeneticPublished by: -
3Staff View
ISSN: 1432-2048Keywords: Aleurone ; (1→3,1→4)-β-Glucanase ; Hordeum (gene regulation) ; Hybridization histochemistry ; Scutellum ; Seed germinationSource: Springer Online Journal Archives 1860-2000Topics: BiologyNotes: Abstract Expression sites of genes encoding (1→3,1→4)-β-glucan 4-glucanohydrolase (EC 3.2.1.73) have been mapped in germinated barley grains (Hordeum vulgare L.) by hybridization histochemistry. A32P-labelled cDNA (copy DNA) probe was hybridized to cryosections of intact barley grains to localize complementary mRNAs. No mRNA encoding (1→3,1→4)-β-glucanase is detected in ungerminated grain. Expression of (1→3,1→4)-β-glucanase genes is first detected in the scutellum after 1 d and is confined to the epithelial layer. At this stage, no expression is apparent in the aleurone. After 2 d, levels of (1→3,1→4)-β-glucanase mRNA decrease in the scutellar epithelium but increase in the aleurone. In the aleurone layer, induction of (1→3,1→4)-β-glucanase gene expression, as measured by mRNA accumulation, progresses from the proximal to distal end of the grain as a front moving away from, and parallel to, the face of the scutellum.Type of Medium: Electronic ResourceURL: -
4Staff View
ISSN: 1615-6102Keywords: Cell surface ; Cryptophyceae ; Freeze fracture/etch ; Periplast ; Scales ; Self-assemblySource: Springer Online Journal Archives 1860-2000Topics: BiologyNotes: Summary The periplast ofHemiselmis brunnescens Butcher is a complex cell covering comprised of the plasma membrane (PM) sandwiched between a surface periplast component (SPC) and an inner periplast component (IPC). The SPC is revealed by deep-etching, and consists of hexagonal plates composed of tripartite subunits that appear to self-assemble into a crystalline layer with a hexagonal symmetry. Small scales (termed fibrillar scales) accumulate on the crystalline plates during cell growth, eventually forming a “carpet” that itself may appear crystalline when fully formed. Heptagonal “rosette scales” are occasionally observed on the surface as well. The position of the crystalline plates is precisely mirrored by both the E and P fracture faces of the PM. The plate proper is underlain by membrane with a high concentration of intramembrane particles (IMPs) while the bands of membrane underlying the plate borders lack IMPs. Access of subunits and fibrillar scales to the cell surface following initial plate formation appears to be at the plate boundaries. This study suggests that cryptomonad flagellates may provide model systems for studying the self-assembly of cell surface components, and for relating membrane structure to function, as evidence suggests a major role for the PM in mediating periplast assembly and development.Type of Medium: Electronic ResourceURL: -
5Staff View
ISSN: 1615-6102Keywords: Flagellar regeneration ; Golgi apparatus ; Green algae ; Membrane flow ; Scale biogenesis ; Scherffelia dubiaSource: Springer Online Journal Archives 1860-2000Topics: BiologyNotes: Summary Cells ofScherffelia dubia regenerate flagella with a complete scale covering after experimental flagellar amputation. Flagellar regeneration was used to study Golgi apparatus (GA) activity during flagellar scale production. By comparing the number of scales present on mature flagella with the flagellar regeneration kinetics, it is calculated that each cell produces ca. 260 scales per minute during flagellar regeneration. Flagellar scales are assembled exclusively in the GA and abstricted from the rims of thetrans-most GA cisternae into vesicles. Exocytosis of scales occurs at the base of the anterior flagellar groove. The central portion of thetrans-most cisterna, containing no scales, detaches from the stack of cisternae and develops a coat to become a coated polygonal vesicle. Scale biogenesis involves continuous turnover of GA cisternae, and scale production rates indicate maturation of four cisternae per minute from each of the cells two dictyosomes. A possible model of membrane flow routes during flagellar regeneration, which involves a membrane recycling loop via the coated polygonal vesicles, is presented.Type of Medium: Electronic ResourceURL: -
6Staff View
ISSN: 1615-6102Keywords: Flagellar regeneration ; Prasinophyceae ; Pyramimonas scalesSource: Springer Online Journal Archives 1860-2000Topics: BiologyNotes: Summary During regeneration of mechanically amputated flagella, flagellar scales and the subtending membrane accumulate in a villiform scale reservoir in which the scales interact to form patterns on the villi reminiscent of the arrangement they later assume on the flagellum. The reservoir membrane is continuous with the plasmalemma, and the scales, attached directly and indirectly to the membrane, leave the reservoir and migrate toward the developing flagella where they assemble into highly ordered layers. It is proposed that scale-scale interactions induce a process of auto-assembly initiating the complex arrangement of scale tiers on the flagellum and cell body.Type of Medium: Electronic ResourceURL: -
7Staff View
ISSN: 1615-6102Keywords: Cell wall ; Golgi apparatus ; Green Algae ; Membrane flow ; Scales ; Scherffelia ; Self-assembly ; ThecaSource: Springer Online Journal Archives 1860-2000Topics: BiologyNotes: Summary Secretion of the cell wall (theca) in the scaly green flagellateScherffelia dubia (Prasinophyceae) has been examined by electron microscopy during cytokinesis. The bi-laminate wall forms by the extracellular amalgamation of two layers of scales produced in the Golgi apparatus (GA). Each mature GA cisterna contains ca. 12,000 scales of two distinct varieties arranged in two layers on the cisternal membrane. GA cisternae undergo turnover and one scale containing cisterna matures from thetransface of each dictyosome every 3–4 minutes. Cisternae then fuse with the plasma membrane at the anterior end of the cell releasing the scales onto the cell surface. The two layers of wall scales integrate on the cell surface in a time-dependent self-assembly process. The first scales deposited commence assembly at the cell posterior and the wall develops anteriorly by edge growth. The daughter cell wall is composed of ca. 1.2 million scales deposited in about 3 hours. Calculations of net membrane flow strongly indicate extensive endocytosis during wall deposition.Type of Medium: Electronic ResourceURL: -
8Staff View
ISSN: 1615-6102Keywords: Prasinophyceae ; Pyramimonas ; MitochondrionSource: Springer Online Journal Archives 1860-2000Topics: BiologyNotes: Summary A serial reconstruction ofPyramimonas gelidicola McFadden, Moestrup andWetherbee has revealed a large reticulated mitochondrion branching throughout the cell. The possibility of single mitochondria in other members of thePrasinophyceae and the uniformity of the morphology of this organelle within the class is discussed.Type of Medium: Electronic ResourceURL: -
9Staff View
ISSN: 1615-6102Keywords: Immunocytochemistry ; Centrin ; Ca2-modulated contractile protein ; Flagellar apparatus ; Green algae ; Fibrous flagellar rootsSource: Springer Online Journal Archives 1860-2000Topics: BiologyNotes: Summary The two main types of fibrous flagellar roots present in the flagellar apparatus of green algae (system I and system II fibers) are immunologically distinct as indicated by the localization of a Ca2+-modulated contractile protein (centrin) exclusively in one type (system II fibers) but not in the other type (system I fibers). A polyclonal antibody generated against the major protein of the striated flagellar roots (system II fibers) of the quadriflagellate green algaTetraselmis striata was used to localize centrin by immunofluorescence and pre- and postembedding immunogold electron microscopy in the flagellar apparatus ofSpermatozopsis similis, S. exsultans, Chlamydomonas reinhardtii, Dunaliella bioculata, Polytomella parva and gametes ofMonostroma grevillei andEnteromorpha sp. Whereas the antibody recognizes centrin in connecting fibers and system II fibers, no labeling occurs in system I fibers in all taxa investigated. This study presents the first evidence that system I fibers lack centrin and indicates that the two main types of fibrous flagellar roots in green algae are biochemically distinct.Type of Medium: Electronic ResourceURL: -
10Staff View
ISSN: 1615-6102Keywords: Flagellar apparatus ; Microtubular cytoskeleton ; Phylogeny ; Prasinophyceae ; PyramimonasSource: Springer Online Journal Archives 1860-2000Topics: BiologyNotes: Summary The absolute configuration of the flagellar apparatus inPyramimonas gelidicola McFadden et al. has been determined and shows identity withP. obovata, indicating that they are closely related. Comparison with the flagellar apparatus of quadriflagellate zoospores from the more advancedChlorophyceae suggest thatPyramimonas may be a primitive ancestral form. The microtubular cytoskeleton has been examined in detail and is shown to be unusual in that it does not attach to the flagellar apparatus. Cytoskeletal microtubules are nucleated individually, and this is interpreted as an adaptation to the methods of mitosis and scale deployment. In view of the primitive nature of these processes, it is proposed that this type of cytoskeletal organization may represent a less advanced condition than that of the flagellar root MTOCs (microtubule organizing centers) observed in theChlorophyceae.Type of Medium: Electronic ResourceURL: -
11Staff View
ISSN: 1615-6102Keywords: Nucleic acid cytochemistry ; Nuclear protrusion ; Pyrenoid ; Rhodella maculata ; Structural RNA ; Ribosomal RNASource: Springer Online Journal Archives 1860-2000Topics: BiologyNotes: Summary Protrusions of the nucleus that extend into the pyrenoid of the unicellular red algaRhodella maculata have been characterised morphologically and cytochemically. Serial reconstructions indicate that cells frequently have two tubular nuclear protrusions that are up to 1.2 μm long. Cytochemical analyses were undertaken to investigate the nucleic acid content of the protrusions. DNA was not detected in the nuclear protrusions, though clear labelling was seen in all other DNA-containing zones (viz. the main nuclear compartment, the chloroplast and the mitochondria). High concentrations of RNA were observed in the nuclear protrusion. In situ hybridization experiments indicate that ribosomal RNAs are not a major component of the protrusion RNA. Possible roles of the protrusion and its RNA content are discussed.Type of Medium: Electronic ResourceURL: -
12Staff View
ISSN: 1615-6102Keywords: Actin ; Apedinella ; Centrin ; Cytoskeleton ; Motility ; Tubulin (Microtubules)Source: Springer Online Journal Archives 1860-2000Topics: BiologyNotes: Summary Motile unicells ofApedinella radians have the extraordinary ability to instantaneously reorient six elongate spine-scales located on the cell surface. Extracellular striated fibrous connectors (termed microligaments) attach spine-scales to discrete regions of the plasma membrane underlain by intricate cytoplasmic plaques. A complex cytoskeleton is associated with the plaques and appears responsible for spine-scale movement. Three cytoskeletal proteins have thus far been identified by immunofluorescence using anti-tubulin, anti-actin, and anti-centrin. The three-dimensional configuration of the cytoskeleton has been established and consists of filamentous bundles of actin and centrin which form stellate systems interconnecting the plaques. Additionally, there is a network of microtubular triads which originate on the surface of the nuclear envelope and subtend the plasma membrane and also support several tentacular protrusions. It is proposed that contraction of the actin and/or centrin filamentous bundles is responsible for the reorientation of the spine-scales.Type of Medium: Electronic ResourceURL: -
13Hofmann, C. J. B. ; Rensing, S. A. ; Häuber, M. M. ; Martin, W. F. ; Müller, S. B. ; Couch, J. ; McFadden, G. I. ; Igloi, G. L. ; Maier, U. -G.
Springer
Published 1994Staff ViewISSN: 1617-4623Keywords: Cryptomonads ; Periplastidal ; Hsp70 ; TransportSource: Springer Online Journal Archives 1860-2000Topics: BiologyNotes: Abstract Cryptomonads are unicellular algae with plastids surrounded by four membranes. Between the two pairs of membranes lies a periplastidal compartment that harbours a DNA-containing organelle, termed the nucleomorph. The nucleomorph is the vestigial nucleus of a phototrophic, eukaryotic endosymbiont. Subcloning of parts of one nucleomorph chromosome revealed a gene coding for an Hsp70 protein. We demonstrate the expression of this nucleomorph protein-coding gene and present a model for protein transport from the host to the endosymbiont compartment.Type of Medium: Electronic ResourceURL: -
14Staff View
ISSN: 0886-1544Keywords: Spermatozopsis ; flagellar roots ; rhizosyndesmos ; Life and Medical Sciences ; Cell & Developmental BiologySource: Wiley InterScience Backfile Collection 1832-2000Topics: BiologyMedicineNotes: The cytoskeleton of the naked, biflagellate green alga Spermatozopsis similis Preisig & Melkonian was isolated by treatment of cells with Nonidet P-40 (0.1%) in lysis buffer (30 mM HEPES, 5 mM EGTA, 15 mM KCl, pH 7) and studied in detail by whole-mount electron microscopy. Isolated cytoskeletons retain the twisted shape of live cells and consist of the two axonemes, the basal apparatus with 4 microtubular and two fibrous roots, and 8-10 secondary cytoskeletal microtubules (SCMT's). The four microtubular flagellar roots differ in number of microtubules (two types with 2 or 5 microtubules, respectively), in their association with fibrous roots of the system I-type (two-stranded roots), in total length (two roots with an average of 4.5 μm and two roots with and average of 7.5 μm), and in length of individual root microtubules. Certain of the root microtubules and most of the SCMT's extend to the posterior end of the cell where they converge, terminate and are interconnected by a fibrous cap-like structure, the rhizosyndesmos. This novel structure consists of a network of 2 nm filaments that presumably lacks centrin as indicated by double immunofluorescence (anti-α-tubulin and anti-centrin) of isolated cytoskeletons. Two-dimensional gel electrophoresis of isolated, purified basal apparatuses of S. similis identifies among other proteins two isoforms of centrin and α- and β-tubulin as intrinsic components.Additional Material: 13 Ill.Type of Medium: Electronic ResourceURL: