STUDIES ON THE LIFE CYCLE AND TAXONOMY OF LIGNIERA VERRUCOSA

Miller , Charles E. (A. and M. College of Texas, College Station.) Studies on the life cycle and taxonomy of Ligniera verrucosa. Amer. Jour. Bot. 46(10): 725–729. Illus. 1959.—A study of the roots of Veronica persica Poir. and V. hederaefolia L. plants infected with Sorosphaera veronicae Schroeter revealed intracellular cystosori and zoosporangial sori of Ligniera verrucosa. The zoosporangial phase of this species has been heretofore unknown. The plasmodia of L. verrucosa occur in root hairs, and other epidermal and sub-epidermal cells of the roots. Zoosporangial and cystosoral plasmodia are indistinguishable until cleavage has started. It is thought that plasmodia produced during early infection develop into zoosporangia, while those produced later develop into resting spores. Zoospores discharged from zoosporangia may reinfect host cells developing there into zoosporangial or cystosoral plasmodia. No evidence for any sexual process was observed. The spherical zoosporangia making up a single zoosporangial sorus may be interconnected; a single discharge pore may serve to liberate zoospores from different zoosporangia. In the Plasmodiophorales the classical basis for generic distinction has been the arrangement of the resting spores in the sorus. Ligniera, because of the supposedly uncharacteristic nature of its cystosori, has been suggested as a host-variety of Sorosphaera. A comparative study of the cystosori and zoosporangia of Ligniera and Sorosphaera growing in a single host has led to the conclusion that these genera should be considered distinct.     

A study of the hatching process in aquatic invertebrates. XVI. Events of eclosion in Calopsectra neoflavellus Malloch (Diptera,Tendipedidae). XVII. Hatching in Argulus megalops Smith (Crustacea,Branchiura)

Summary Hatching in the tendipedid, Calopsectra neoflavellus involves first a slow uptake of water by the embryo during development, whereby it increases in size and comes to fill entirely the space within the chorion. After completion of embryonic development, the prolarva increases still more in size by swallowing and absorbing water. Internal pressure thus generated results in the bursting of the chorion. The larva then frees itself by active movements.In the branchiuran, Argulus megalops, hatching is similar to that previously described for Copepoda, in that an inner egg membrane swells osmotically and splits the outer chorion. Subsequent bursting of the inner membrane throws the larva nearly out of the egg, but final emergence is by active struggle of the larva.

---

Zusammenfassung Das Ausschlüpfen von Calopsectra neoflavellus enthält erstens eine langsame Wasseraufnahme durch den Embryo, wodurch der Embryo wächst und das Wasser den ganzen Raum zwischen Embryo und Chorion füllt. Nach Vollendung der Entwicklung quillt der Embryo noch mehr auf durch den Schluckakt und Aufnahme des Wassers. Dann zerreisst das Chorion durch den intraovularen Druck. Endlich befreit sich die Larve durch Sträuben.In Argulus megalops (Branchiura) gleicht das Ausschlüpfen dem vorher dargestellten für den Copepoden. Eine innere Membran schwillt osmotisch und zerreisst; das Chorion dann zerreist auch die innere Membran selbst and wirft die Larve nahezu aus dem Ei hinaus, aber die schliessiiche Befreiung geschieht durch Sträuben.

---

---

Supported by National Science Foundation grant GB-219, entitled A study of hatching and of the ecology of egg masses of aquatic invertebrates.     

Secretion of the sweet-tasting plant protein thaumatin byStreptomyces lividans

Summary To produce and direct the export inStreptomyces lividans of the sweet plant protein thaumatin, thaumatin II cDNA was fused in the correct reading frame to the -galactosidase leader peptide, under the control of the -galactosidase promoter and ribosome binding site. The export of the recombinant thaumatin may allow the correct formation of the thaumatin disulfide bonds. The recombinant thaumatin was purified from the medium on an S-Sepharose column and detected with western blots by sheep -thaumatin antibodies. The recombinant thaumatin was the same size as authentic thaumatin and changed position on an acrylamide gel in response to reduction by 2-mercaptoethanol in the same manner.     

The effect of whey protein hydrolyzates on the lactic acid fermentation

Summary The batch fermentation of whey permeate to lactic acid was improved markedly by the addition of enzymehydrolyzed whey protein. Acid concentrations greater than 90 g/l were achieved at a productivity of 4.3 g/l per h and a 98% substrate use. Cell mass concentration reached 6 g/l. The acid productivity achieved is somewhat higher than that typical for fermentation of whole whey. The process economics, based on in-house hydrolyzate preparation, look promising. Presented in this paper are the experimental results showing the effects of hydrolyzate concentration on acid and cell mass production.     

Sites of Tubulin Polymerization in PC 12 Cells

The site at which tubulin enters into polymer in the neuritic process is a very important datum in terms of our understanding of the mechanism of transport of the microtubular cytoskeleton out the axon. If the form of tubulin being transported out the axon is the microtubule, then assembly of tubulin into microtubules should occur at or near the cell body; if, however, the form of tubulin transported is free tubulin dimer, then assembly can occur at any free microtubule end out the neurite. We have injected a fluorescent analog of tubulin into differentiated PC 12 cells and used differential extraction protocols to extract free dimer but not microtubules. We have imaged these cells before and after extraction by low-light-level video fluorescence microscopy and have used image analysis to examine the sites of tubulin incorporation into polymer or other unextracted components as a function of time. We find that tubulin in the distal reaches of the neurite is found initially as monomer and that its appearance in the unextracted component occurs later. This pattern of appearance of fluorescent tubulin initially in the soluble fraction and later in the unextractable component is qualitatively similar to that reported by other workers for biotinylated tubulin, but we see a larger gap between the rates of appearance in soluble fraction and in polymer. Quantitative analysis of fluorescence intensities in the two compartments with distance out the neurite reveals substantial variation between different neurites: In some neurites, the pattern of variation of unextracted/total tubulin suggests that tubulin enters into the unextracted component primarily near the cell body and that this unextracted component moves out the neurite with time, and in other neurites it suggest that monomer adds into microtubule ends staggered out the neurite. In no case do we see a pattern suggesting that distal addition predominates. These analyses of fluorescence intensities in extracted and unextracted neurites suggest that both transport of polymerized microtubules and monomer addition onto staggered microtubule ends occur in PC12 neurites and that in individual neurites one or the other of these two behaviors may predominate.     

Control of Globodera tabacum solanacearum by Alternating Host Resistance and Nematicide

The feasibility of alternating use of resistant vs. susceptible flue-cured tobacco cultivars to improve control of Globodera tabacum subsp, solanacearum (TCN) was investigated at two Virginia locations in 1984-86. Post-harvest TCN population densities were reduced in each year of the study when fenamiphos was used with a TCN-resistant cultivar (NC 567), relative to susceptible cultivars (K 326 or Mc 944). Using NC 567 with fenamipbos also reduced preplant TCN population densities in the next growing season. Egg population densities before planting in 1986 were significantly lower in plots planted with NC 567 in 1984, even when a susceptible cultivar had been planted in 1985. Use of fenamiphos with NC 567 in 1984 and 1985 further reduced preplant egg population densities in 1986. Economic returns were significantly greater in 1984 when NC 567 was used with fenamiphos, rather than a susceptible cultivar. Treatments involving fenamiphos and (or) NC 567 in 1984 and 1985 resulted in higher economic returns in 1986 than did treatments using a susceptible cultivar without fenamiphos in both previous years. Economic returns were highest in 1986 when fenamiphos and NC 567 were used in 1984 and 1985 and a susceptible cultivar was planted in 1986.     

The three-dimensional structure of bovine platelet factor 4 at 3.0-A resolution

Platelet factor 4 (PF4), which is released by platelets during coagulation, binds very tightly to negatively charged oligosaccharides such as heparin. To date, six other proteins are known that are homologous in sequence with PF4 but have quite different functions. The structure of a tetramer of bovine PF4 complexed with one Ni(CN)4(2-) molecule has been determined at 3.0 A resolution and refined to an R factor of 0.28. The current model contains residues 24-85, no solvent, and one overall temperature factor. Residues 1-13, which carried an oligosaccharide chain, were removed with elastase to induce crystallization; residues 14-23 and presumably 86-88 are disordered in the electron density map. Because no heavy atom derivative was isomorphous with the native crystals, the complex of PF4 with one Ni(CN)4(2-) molecule was solved using a single, highly isomorphous Pt(CN)4(2-) derivative and the iterative, single isomorphous replacement method. The secondary structure of the PF4 subunit, from amino- to carboxyl-terminal end, consists of an extended loop, three strands of antiparallel beta-sheet arranged in a Greek key, and one alpha-helix. The tetramer contains two extended, six-stranded beta-sheets, each formed by two subunits, which are arranged back-to-back to form a "beta-bilayer" structure with two buried salt bridges sandwiched in the middle. The carboxyl-terminal alpha-helices, which contain lysine residues that are thought to be intimately involved in binding heparin, are arranged as antiparallel pairs on the surface of each extended beta-sheet.