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Biomedical subjects

M A Yund

Publications and source records attributed to M A Yund.

10 recordsLinked to original sources

Mechanisms of plant embryo development.

1. Evolution in plants has favored both a simpler body plan with fewer cell types and the epigenetic flexibility to regenerate, via growth, dedifferentiation, and redifferentiation, to recover from environmental insults. It has become increasingly apparent that a plant cell uses external signals to differentiate and to maintain or to change the differentiated state. A cell-cell signaling and positional information strategy seems to be the predominant mechanism employed in plant development. 2. An axis can be initiated by physical/chemical forces such as light and ion current, requiring no new gene action. Random chemical fluctuations and physicochemical forces could explain the initiation of differences among cells of equal developmental potential. Amplification of chemical polarizing events may lead to biochemical differences, new gene expression, and finally shoot/root axis establishment. 3. Radial and axial patterning may be governed by a mechanism involving polar auxin transport. 4. Because the meristems and the three fundamental tissues formed during embryogenesis are renewed and extended throughout the life of the plant, with some exceptions, most genes expressed in the embryo are also expressed during postgermination development. 5. Embryogenic competence is acquired during reproductive development. While the zygote is determined for embryogenesis, the developing embryo and often the seedling remain embryogenic. Embryogenic potential declines during vegetative development. The embryogenic strength of a tissue is correlated with its developmental distance from the zygote.

Embryonic Induction↗

Ecdysteroid binding activity in embryos of Drosophila melanogaster.

Ecdysteroid binding proteins have been found in nuclei of Drosophila melanogaster embryos. Comparison of results derived from Scatchard analysis, analogue binding competition, and sucrose gradient centrifugation has revealed no significant differences between the properties of the putative embryonic receptor and those of the receptor found in imaginal disks or Kc cells.

Animals↗

Specific binding of 20-hydroxyecdysone to nuclei of imaginal discs of Drosophila melanogaster.

Specific binding of the insect steroid hormone 20-hydroxyecdysone to imaginal discs of Drosophila melanogaster has been investigated. Evidence is presented showing that most of the specific binding is located in the nuclear fraction at the time changes in gene function are observed. Nuclear binding is high affinity, analog specific, apparently saturable, and unaffected by inhibitors of RNA and protein synthesis. The association kinetics of nuclear binding are very similar to those of specific binding in whole cells. Specific binding to whole discs and to disc nuclei is temperature-dependent, but equal levels of nuclear binding are achieved after 1 h at 25 degrees C and 8 h at 0-4 degrees C. There is little or no lag in the nuclear location of specific binding at either temperature. The biochemical properties of the specific nuclear binding are consistent with the involvement of these sites in the hormone detection and response system mediating imaginal disc morphogenesis.

Amanitins↗

Ecdysteroid receptors in imaginal discs of Drosophila melanogaster.

[3H]Ponasterone A (PNA) of high specific activity has been used to identify and begin characterization of ecdysteroid (formerly called ecdysone) receptors in cytoplasmic and nuclear fractions of imaginal discs of Drosophila melanogaster. The equilibrium Kd of the observed macromolecular binding, 3--4 X 10(-9) M PNA, is in good agreement with the minimal concentration required for induction of complete morphogenesis in vitro, 4.2 X 10(-9) M PNA. Binding is analog specific and has kinetics consistent with a role in hormone response. On gentle homogenization, less than 5% of the binding capacity of the cell is released as soluble receptor; the other 95% remains with the nuclear fraction. This nuclear fraction specifically binds [3H]PNA in vitro. Greater than 95% of nuclear PNA receptors are released by extraction with 0.3 M KCl. The binding properties of the nuclear receptors are indistinguishable from those of the cytosol fraction or of the whole cell.

Animals↗