Cell and nucleomorph division in the alga Cryptomonas

1982 ◽  
Vol 60 (11) ◽  
pp. 2440-2452 ◽  
Author(s):  
Lisa McKerracher ◽  
Sarah P. Gibbs
Keyword(s):  
Endoplasmic Reticulum ◽  
Nuclear Envelope ◽  
Outer Membrane ◽  
Basal Body ◽  
Nuclear Division ◽  
Residual Nucleus ◽  
Inner Membrane ◽  
Double Membrane ◽  
Ultrastructural Investigation ◽  
Periplastidal Compartment

An ultrastructural investigation of cell and nuclear division in Cryptomonas sp. (θ) was made with particular emphasis on the mode of division of the chloroplast and nucleomorph. Mitosis is similar to that in other cryptomonads except that the nuclear envelope remains mostly intact. Division of the single chloroplast occurs in preprophase by constriction through the dorsal bridge. Frequently there is a lag between the division of the chloroplast and the division of its envelope of chloroplast endoplasmic reticulum. In addition, the inner membrane of the chloroplast endoplasmic reticulum may infold well in advance of the outer membrane.The nucleomorph is a unique double membrane limited organelle which is found in the periplastidal compartment of cryptomonads. It divides in preprophase following basal body replication but before division of the chloroplast and its chloroplast endoplasmic reticulum is complete. The inner membrane of the nucleomorph envelope invaginates first forming a double membraned baffle. The outer membrane invaginates next and completes division. Microtubules are not involved in nucleomorph division. None were observed and colchicine, which inhibited nuclear division, did not inhibit nucleomorph division. The theory that the nucleomorph is the residual nucleus of a former eukaryotic endosymbiont is reevaluated in light of these new observations.

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 nuclear envelope

2019 ◽  
pp. 140-146
Author(s):  
John C. Lucchesi
Keyword(s):  
Nuclear Envelope ◽  
Lipid Bilayers ◽  
Nuclear Membrane ◽  
Substantial Portion ◽  
Inner Membrane ◽  
Double Membrane ◽  
Stochastic Nature ◽  
Inner Surface ◽  
Associated Proteins ◽  
Or Gene

The nuclear envelope is a double membrane sheath made up of two lipid bilayers—an outer and an inner membrane. The inner surface of the inner membrane is associated with a meshwork of filaments made up of lamins and of lamin-associated proteins that constitute the lamina. A substantial portion of the genome contacts the lamina through lamina-associated domains (LADs). LADs usually position silent or gene-poor regions of the genome near the lamina and nuclear membrane. The position of some LADs is different in some cells of the same tissue, reflecting the stochastic nature of gene activity; it can also change during differentiation, allowing the necessary activation of particular genes. Contact of transcription units with nuclear pores can result in activation or, sometimes, repression. Some of the proteins that contribute to the structure of the pores can activate transcription by associating with genes or with super-enhancers away from the nuclear membrane.

scholarly journals Nuclear Envelope Proteins Modulating the Heterochromatin Formation and Functions in Fission Yeast

Cells ◽  
2020 ◽  
Vol 9 (8) ◽  
pp. 1908 ◽  
Author(s):  
Yasuhiro Hirano ◽  
Haruhiko Asakawa ◽  
Takeshi Sakuno ◽  
Tokuko Haraguchi ◽  
Yasushi Hiraoka
Keyword(s):  
Endoplasmic Reticulum ◽  
Nuclear Envelope ◽  
Fission Yeast ◽  
Histone Deacetylase ◽  
Nuclear Pore Complex ◽  
Molecular Mechanisms ◽  
Nuclear Pore ◽  
Double Membrane ◽  
Heterochromatin Formation ◽  
Nuclear Membranes

The nuclear envelope (NE) consists of the inner and outer nuclear membranes (INM and ONM), and the nuclear pore complex (NPC), which penetrates the double membrane. ONM continues with the endoplasmic reticulum (ER). INM and NPC can interact with chromatin to regulate the genetic activities of the chromosome. Studies in the fission yeast Schizosaccharomyces pombe have contributed to understanding the molecular mechanisms underlying heterochromatin formation by the RNAi-mediated and histone deacetylase machineries. Recent studies have demonstrated that NE proteins modulate heterochromatin formation and functions through interactions with heterochromatic regions, including the pericentromeric and the sub-telomeric regions. In this review, we first introduce the molecular mechanisms underlying the heterochromatin formation and functions in fission yeast, and then summarize the NE proteins that play a role in anchoring heterochromatic regions and in modulating heterochromatin formation and functions, highlighting roles for a conserved INM protein, Lem2.

scholarly journals Distribution and induction of cytochrome P-450 in rat liver nuclear envelope.

1981 ◽  
Vol 91 (1) ◽  
pp. 212-220 ◽  
Author(s):  
S Matsuura ◽  
R Masuda ◽  
K Omori ◽  
M Negishi ◽  
Y Tashiro
Keyword(s):  
Nuclear Envelope ◽  
Outer Membrane ◽  
Rat Liver ◽  
Molecular Species ◽  
Transmembrane Protein ◽  
Microscopic Analysis ◽  
Inner Membrane ◽  
Cytoplasmic Face ◽  
Biochemical Analyses ◽  
Cytochrome P 450

Induction of cytochrome P-450s by 3-methylcholanthrene (MC) and phenobarbital (PB) and distribution of P-450s in the rat liver nuclear envelope were investigated by biochemical analyses and ferritin immunoelectron microscopy using specific antibodies against the major molecular species of MC- and PB-induced cytochrome P-450. It was found, in agreement with Kasper (J. Biol. Chem., 1971, 246: 577-581), that the total amount of cytochrome P-450s determined by biochemical analysis was markedly increased by MC, but not by PB, treatment. Immunoelectron microscopic analysis, however, showed marked and slight increases in ferritin labeling by MC and PB treatment, respectively. The latter finding was interpreted as resulting from the induction of a particular molecular species of PB-induced cytochrome P-450s. Ferritin immunoelectron microscopic analysis of intact isolated nuclei, naked nuclei from which the outer membrane of the nuclear envelope was partially detached (mechanically), and isolated nuclear envelopes have shown that the ferritin particles are found exclusively on the cytoplasmic face of the outer nuclear envelopes. Neither the nucleoplasmic face of the inner membrane of the nuclear envelope nor the cisternal face of both membranes of the nuclear envelope showed any labeling with ferritin. This indicates that cytochrome P-450 is located only on the outer membrane of the nuclear envelope and does not diffuse laterally into the domain of the inner membrane of the nuclear envelope across the nuclear pores. Our results suggest that a marked heterogeneity exists in the enzyme distribution between the outer and inner membrane of the nuclear envelope and that microsomal marker enzymes such as cytochrome P-450 exist exclusively in the outer membrane. In addition, it appears that cytochrome P-450 is probably not a transmembrane protein but an intrinsic protein located on the cytoplasmic face of the outer membrane of the nuclear envelope.

scholarly journals Casting a Wider Net: Differentiating between Inner Nuclear Envelope and Outer Nuclear Envelope Transmembrane Proteins

2019 ◽  
Vol 20 (21) ◽  
pp. 5248 ◽  
Author(s):  
Mark Tingey ◽  
Krishna C. Mudumbi ◽  
Eric C. Schirmer ◽  
Weidong Yang
Keyword(s):  
Endoplasmic Reticulum ◽  
Nuclear Envelope ◽  
Nuclear Membrane ◽  
Nuclear Organization ◽  
Transmembrane Proteins ◽  
Eukaryotic Cells ◽  
Genome Architecture ◽  
Double Membrane ◽  
Vital Functions ◽  
Nuclear Stability

The nuclear envelope (NE) surrounds the nucleus with a double membrane in eukaryotic cells. The double membranes are embedded with proteins that are synthesized on the endoplasmic reticulum and often destined specifically for either the outer nuclear membrane (ONM) or the inner nuclear membrane (INM). These nuclear envelope transmembrane proteins (NETs) play important roles in cellular function and participate in transcription, epigenetics, splicing, DNA replication, genome architecture, nuclear structure, nuclear stability, nuclear organization, and nuclear positioning. These vital functions are dependent upon both the correct localization and relative concentrations of NETs on the appropriate membrane of the NE. It is, therefore, important to understand the distribution and abundance of NETs on the NE. This review will evaluate the current tools and methodologies available to address this important topic.

Compound Symbiosis in Peridinium Balticum

1973 ◽  
Vol 31 ◽  
pp. 500-501
Author(s):  
R. N. Tomas
Keyword(s):  
Endoplasmic Reticulum ◽  
Nuclear Envelope ◽  
The Other ◽  
Exact Nature ◽  
Symbiotic Relationship

Peridinium balticum appears to be unusual among the dinoflagellates in that it possesses two DNA-containing structures as determined by histochemical techniques. Ultrastructurally, the two dissimilar nuclei are contained within different protoplasts; one of the nuclei is characteristically dinophycean in nature, while the other is characteristically eucaryotic. The chloroplasts observed within P. balticum are intrinsic to an eucaryotic photosynthetic endosymbiont and not to the dinoflagellate. These organelles are surrounded by outpocketings of endoplasmic reticulum which are continuous with the eucaryotic nuclear envelope and are characterized by thylakoids composed of three apposed lamellae. Girdle lamellae and membranebounded interlamellar pyrenoids are also present. Only the plasmalemma of the endosymbiont segregates its protoplast from that of the dinophycean cytoplasm. The exact nature of this symbiotic relationship is at present not known.

Temporal and spatial interrelationships of confronting cisternae to nuclear envelope

1992 ◽  
Vol 50 (1) ◽  
pp. 930-931
Author(s):  
John R. Palisano
Keyword(s):  
Endoplasmic Reticulum ◽  
Nuclear Envelope ◽  
Tumor Cells ◽  
Hela Cells ◽  
Microscopic Investigation ◽  
Electron Microscopic Investigation ◽  
Serial Sections ◽  
Electron Microscopic ◽  
Fetal Rat ◽  
Temporal And Spatial

Although confronting cistemae (CC) have been observed in a variety of tumor cells and normal fetal rat, mouse, and human epithelial tissues, little is known about their origin or role in mitotic cells. While several investigators have suggested that CC arise from nuclear envelope (NE) folding back on itself during prophase, others have suggested that CC arise when fragments of NE pair with endoplasmic reticulum. An electron microscopic investigation of 0.25 um thick serial sections was undertaken to examine the origin of CC in HeLa cells.

The ultrastructure of the double membrane-bound bodies and endoplasmic reticulum in serial sections of wheat spot mosaic-affected wheat plants

1990 ◽  
Vol 48 (3) ◽  
pp. 694-695
Author(s):  
M. H. Chen ◽  
C. Hiruki
Keyword(s):  
Endoplasmic Reticulum ◽  
High Resolution ◽  
Membrane Structure ◽  
Mosaic Disease ◽  
Serial Sections ◽  
Thin Sections ◽  
Double Membrane ◽  
Southern Alberta ◽  
Membrane Bound ◽  
Scanning Em

Wheat spot mosaic disease was first discovered in southern Alberta, Canada, in 1956. A hitherto unidentified disease-causing agent, transmitted by the eriophyid mite, caused chlorosis, stunting and finally severe necrosis resulting in the death of the affected plants. Double membrane-bound bodies (DMBB), 0.1-0.2 μm in diameter were found to be associated with the disease.Young tissues of leaf and root from 4-wk-old infected wheat plants were fixed, dehydrated, and embedded in Spurr’s resin. Serial sections were collected on slot copper grids and stained. The thin sections were then examined with a Hitachi H-7000 TEM at 75 kV. The membrane structure of the DMBBs was studied by numbering them individually and tracing along the sections to see any physical connection with endoplasmic reticulum (ER) membranes. For high resolution scanning EM, a modification of Tanaka’s method was used. The specimens were examined with a Hitachi Model S-570 SEM in its high resolution mode at 20 kV.

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