scholarly journals AN UNUSUAL MITOTIC MECHANISM IN THE PARASITIC PROTOZOAN SYNDINIUM SP

1974 ◽  
Vol 60 (3) ◽  
pp. 702-720 ◽  
Author(s):  
Hans Ris ◽  
Donna F. Kubai
Keyword(s):  
Nuclear Envelope ◽  
Nuclear Division ◽  
Specific Area ◽  
Nuclear Space ◽  
Dense Layer ◽  
Nuclear Surface ◽  
Free Living ◽  
Central Spindle ◽  
Cytoplasmic Channel ◽  
Sister Kinetochore

Syndinium and related organisms which parasitize a number of invertebrates have been classified with dinoflagellates on the basis of the morphology of their zoospores. We demonstrate here that with respect to chromosome structure and chemistry as well as nuclear division, they differ fundamentally from free-living dinoflagellates. Alkaline fast green staining indicates the presence of basic proteins in Syndinium chromosomes. Chromatin fibers are about 30 Å thick and do not show the arrangement characteristic of dinoflagellate chromosomes. The four V-shaped chromosomes are permanently attached at their apexes to a specific area of the nuclear membrane through a kinetochore-like trilaminar disk inserted into an opening of the membrane. Microtubules connect the outer dense layer of each kinetochore to the bases of the two centrioles located in a pocket-shaped invagination of the nuclear envelope. During division kinetochores duplicate, and each sister kinetochore becomes attached to a different centriole. As the centrioles move apart, apparently pushed by a bundle of elongating microtubules (central spindle), the daughter chromosomes are passively pulled apart. During the process of elongation of the central spindle, the cytoplasmic groove on the nuclear surface which contains the central spindle sinks into the nuclear space and is transformed into a cylindrical cytoplasmic channel. A constriction in the persisting nuclear envelope leads to the formation of two daughter nuclei.

Detection and mapping of interactions between chromatin and the nuclear envelope in drosophila embryos

1995 ◽  
Vol 53 ◽  
pp. 764-765
Author(s):  
W.F. Marshall ◽  
A.F. Dernburg ◽  
B. Harmon ◽  
J.W. Sedat
Keyword(s):  
Nuclear Envelope ◽  
Chromatin Condensation ◽  
Three Dimensional ◽  
Physiological Role ◽  
Nuclear Surface ◽  
Intact Cells ◽  
Molecular Determinants ◽  
Surface Harmonic ◽  
Drosophila Embryos

Interactions between chromatin and nuclear envelope (NE) have been implicated in chromatin condensation, gene regulation, nuclear reassembly, and organization of chromosomes within the nucleus. To further investigate the physiological role played by such interactions, it will be necessary to determine which loci specifically interact with the nuclear envelope. This will not only facilitate identification of the molecular determinants of this interaction, but will also allow manipulation of the pattern of chromatin-NE interactions to probe possible functions. We have developed a microscopic approach to detect and map chromatin-NE interactions inside intact cells.Fluorescence in situ hybridization (FISH) is used to localize specific chromosomal regions within the nucleus of Drosophila embryos and anti-lamin immunofluorescence is used to detect the nuclear envelope. Widefield deconvolution microscopy is then used to obtain a three-dimensional image of the sample (Fig. 1). The nuclear surface is represented by a surface-harmonic expansion (Fig 2). A statistical test for association of the FISH spot with the surface is then performed.

scholarly journals Immunochemical and immunocytochemical identification of a myosin heavy chain polypeptide in Nicotiana pollen tubes

1989 ◽  
Vol 92 (4) ◽  
pp. 569-574
Author(s):  
X.J. Tang ◽  
P.K. Hepler ◽  
S.P. Scordilis
Keyword(s):  
Pollen Tube ◽  
Nuclear Envelope ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Immunofluorescence Microscopy ◽  
Generative Cell ◽  
Pollen Tubes ◽  
Nuclear Surface ◽  
Common Pattern ◽  
Western Blots

A myosin heavy chain polypeptide has been identified and localized in Nicotiana pollen tubes using monoclonal anti-myosin antibodies. The epitopes of these antibodies were found to reside on the myosin heavy chain head and rod portion and were, therefore, designated anti-S-1 (myosin S-1) and anti-LMM (light meromyosin). On Western blots of the total soluble pollen tube proteins, both anti-S-1 and anti-LMM label a polypeptide of approximately 175,000 Mr. Immunofluorescence microscopy shows that both antibodies yield numerous fluorescent spots throughout the whole length of the tube, often with an enrichment in the tube tip. These fluorescent spots are thought to represent vesicles and/or organelles in the pollen tubes. In addition to this common pattern, anti-S-1 stains both the generative cell and the vegetative nuclear envelope. The different staining patterns of the nucleus between anti-S-1 and anti-LMM may be caused by some organization and/or anchorage state of the myosin molecules on the nuclear surface that differs from those on the vesicles and/or organelles.

scholarly journals Monoclonal antibodies identify a group of nuclear pore complex glycoproteins.

1987 ◽  
Vol 104 (5) ◽  
pp. 1143-1156 ◽  
Author(s):  
C M Snow ◽  
A Senior ◽  
L Gerace
Keyword(s):  
Monoclonal Antibodies ◽  
Nuclear Envelope ◽  
Nuclear Pore Complex ◽  
Peptide Mapping ◽  
Polyclonal Antibodies ◽  
Integral Membrane Protein ◽  
Nucleocytoplasmic Transport ◽  
Nuclear Pore ◽  
Nuclear Surface ◽  
Punctate Pattern

Using monoclonal antibodies we identified a group of eight polypeptides of rat liver nuclear envelopes that have common epitopes. Most or all of these proteins are structurally distinct, as shown by tryptic peptide mapping and analysis with polyclonal antibodies. While these polypeptides are relatively tightly bound to nuclear membranes, only one is an integral membrane protein. The eight antigens cofractionate with the nuclear pore complex under various conditions of ionic strength and detergent. It can be seen by immunofluorescence microscopy that the monoclonal antibodies reacting with these antigens stain the nuclear surface of interphase cells in a finely punctate pattern. When the nuclear envelope is disassembled and subsequently reformed during mitosis, the proteins are reversibly dispersed throughout the cytoplasm in the form of minute foci. By EM immunogold localization on isolated nuclear envelopes, the monoclonal antibodies label exclusively the nuclear pore complex, at both its nucleoplasmic and cytoplasmic margins. Considered together, our biochemical and localization data indicate that the eight nuclear envelope polypeptides are pore complex components. As shown in the accompanying paper (Holt, G. D., C. M. Snow, A. Senior, R. S. Haltiwanger, L. Gerace, and G. W. Hart, J. Cell Biol., 104:1157-1164) these eight polypeptides contain a novel form of glycosylation, O-linked N-acetylglucosamine. The relative abundance and disposition of these O-linked glycoproteins in the pore complex are consistent with their having a role in nucleocytoplasmic transport.

Nuclear division in the marine dinoflagellate Oxyrrhis marina

1986 ◽  
Vol 85 (1) ◽  
pp. 161-175
Author(s):  
X.P. Gao ◽  
J.Y. Li
Keyword(s):  
Nuclear Envelope ◽  
Phylogenetic Relationships ◽  
Nuclear Division ◽  
Metaphase Plate ◽  
Active Role ◽  
Ultrastructural Changes ◽  
Interphase Nuclei ◽  
Oxyrrhis Marina ◽  
Two Stages ◽  
Anaphase B

The nuclear division of Oxyrrhis marina is a very distinct one among the mitoses of dinoflagellates that have been studies. Using synchronized populations, we have investigated the ultrastructural changes in this nuclear division. In interphase, nuclei can be classified into two groups on the basis of the shapes of the chromosomes. Y- and U-shaped chromosomes have been observed in both types of interphase nuclei. By prophase the nucleus becomes oval, many nuclear plaques appear on the nuclear envelope, and many microtubules radiate from these nuclear plaques within the nucleus. Metaphase can be identified by the characteristic arrangement of the chromosomes; an equatorial metaphase plate is absent. As in many higher organisms, anaphase includes two stages: anaphase A and anaphase B. During anaphase A the nucleus does not apparently elongate and the chromosomes migrate towards the poles by a combination of the shortening of the chromosome-associated microtubules and the elongation of those located between daughter chromosomes. During anaphase B the nucleus elongates to about twice its former length. This elongation may result from growth of the interzonal nuclear envelope. Dividing nucleoli are associated with microtubules, which suggests that microtubules may play an active role in the division of the nucleolus. The evolution of mitosis and the phylogenetic relationships between Oxyrrhis, typical dinoflagellates and Syndinium are discussed.

scholarly journals Mechanical principles of nuclear shaping and positioning

2018 ◽  
Vol 217 (10) ◽  
pp. 3330-3342 ◽  
Author(s):  
Tanmay P. Lele ◽  
Richard B. Dickinson ◽  
Gregg G. Gundersen
Keyword(s):  
Nuclear Envelope ◽  
Mechanical Response ◽  
Mechanical Resistance ◽  
Nuclear Surface ◽  
Nuclear Movement ◽  
Large Size ◽  
Force Transfer ◽  
Nuclear Shaping ◽  
Resistance To Deformation ◽  
Cellular Forces

Positioning and shaping the nucleus represents a mechanical challenge for the migrating cell because of its large size and resistance to deformation. Cells shape and position the nucleus by transmitting forces from the cytoskeleton onto the nuclear surface. This force transfer can occur through specialized linkages between the nuclear envelope and the cytoskeleton. In response, the nucleus can deform and/or it can move. Nuclear movement will occur when there is a net differential in mechanical force across the nucleus, while nuclear deformation will occur when mechanical forces overcome the mechanical resistance of the various structures that comprise the nucleus. In this perspective, we review current literature on the sources and magnitude of cellular forces exerted on the nucleus, the nuclear envelope proteins involved in transferring cellular forces, and the contribution of different nuclear structural components to the mechanical response of the nucleus to these forces.

Ultrastructural changes in nuclear membranes and organelle associations during mitosis of the aquatic fungus Entophlyctis sp.

1975 ◽  
Vol 53 (7) ◽  
pp. 627-646 ◽  
Author(s):  
Martha J. Powell
Keyword(s):  
Endoplasmic Reticulum ◽  
Nuclear Envelope ◽  
Nuclear Division ◽  
Ultrastructural Changes ◽  
Aquatic Fungus ◽  
Electron Microscopic ◽  
Mitotic Apparatus ◽  
Inner Membrane ◽  
Nuclear Membranes ◽  
Spindle Microtubules

Electron microscopic observations on an endobiotic chytrid, Entophlyctis sp., have revealed a mitotic apparatus which is presently unique among fungi. Daughter nuclear envelopes are reconstituted from cisternae apparently proliferated by the inner membrane of the nuclear envelope. Before nuclear division, centrioles replicate and migrate to the poles of the nucleus. Large pores appear at this time in a depression of the nuclear envelope opposite the paired centrioles. This region of the envelope fragments and leaves polar fenestrae as spindle microtubules appear in the nucleus. The inner membrane of the nuclear envelope then invaginates and proliferates cisternae until a layer of inner membrane cisternae lines the original nuclear envelope at late metaphase. Connections between the inner membrane of the original nuclear envelope and the cisternae persist until telophase. As the spindle elongates and the inner membrane cisternae fuse centripetally to form a reticulum around the chromatin mass, the original nuclear envelope opens more at the poles. The reticulum becomes the nuclear envelope of the new daughter nuclei. When the original envelope finally disperses, it is distinguishable from the endoplasmic reticulum only by the presence of pores. Microbodies are consistently associated with the original nuclear envelope and appear adjacent to the new daughter envelopes at the end of telophase. Densely staining arms project from the sides of the primary centrioles toward the polar mitochondria.

The ultrastructure of nuclear division in Armillaria mellea: meiosis

1979 ◽  
Vol 57 (18) ◽  
pp. 1860-1872 ◽  
Author(s):  
Diane Cope Peabody ◽  
Jerome J. Motta
Keyword(s):  
Nuclear Envelope ◽  
Membrane Structure ◽  
Nuclear Division ◽  
Spindle Pole ◽  
Armillaria Mellea ◽  
Spindle Pole Bodies ◽  
Late Telophase ◽  
Meiosis I ◽  
Metaphase I

Meiosis I in isolates of Armillaria mellea in which subhymenial hyphae are uninucleate and lack clamp connections was examined ultrastructurally. Although the overall pattern of development and basidiosporogenesis appears similar to other Homobasidiomycetes it was observed that spindle pole bodies are predominantly monoglobular and are associated with a unique membrane structure of the subtending nuclear envelope. The nuclear envelope also disappears at metaphase I and reforms by the coalescence of membrane fragments around the compacted chromatin at late telophase I. The significance of these features in relation to other Basidiomycetes is briefly discussed.

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