scholarly journals A Homolog of Structural Maintenance of Chromosome 1 Is a Persistent Centromeric Protein Which Associates With Nuclear Pore Components in Toxoplasma gondii

2020 ◽  
Vol 10 ◽  
Author(s):  
Maria E. Francia ◽  
Sheila Bhavsar ◽  
Li-Min Ting ◽  
Matthew M. Croken ◽  
Kami Kim ◽  
...  
Keyword(s):  
Toxoplasma Gondii ◽  
Chromosome 1 ◽  
Nuclear Pore ◽  
Centromeric Protein ◽  
Structural Maintenance Of Chromosome

scholarly journals O-fucosylated glycoproteins form assemblies in close proximity to the nuclear pore complexes of Toxoplasma gondii

2016 ◽  
Vol 113 (41) ◽  
pp. 11567-11572 ◽  
Author(s):  
Giulia Bandini ◽  
John R. Haserick ◽  
Edwin Motari ◽  
Dinkorma T. Ouologuem ◽  
Sebastian Lourido ◽  
...  
Keyword(s):  
Toxoplasma Gondii ◽  
Host Cells ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Signaling Proteins ◽  
Superresolution Microscopy ◽  
Processing Enzymes ◽  
Close Proximity ◽  
Pore Complexes ◽  
Aleuria Aurantia

Toxoplasma gondii is an intracellular parasite that causes disseminated infections in fetuses and immunocompromised individuals. Although gene regulation is important for parasite differentiation and pathogenesis, little is known about protein organization in the nucleus. Here we show that the fucose-binding Aleuria aurantia lectin (AAL) binds to numerous punctate structures in the nuclei of tachyzoites, bradyzoites, and sporozoites but not oocysts. AAL also binds to Hammondia and Neospora nuclei but not to more distantly related apicomplexans. Analyses of the AAL-enriched fraction indicate that AAL binds O-linked fucose added to Ser/Thr residues present in or adjacent to Ser-rich domains (SRDs). Sixty-nine Ser-rich proteins were reproducibly enriched with AAL, including nucleoporins, mRNA-processing enzymes, and cell-signaling proteins. Two endogenous SRDs-containing proteins and an SRD-YFP fusion localize with AAL to the nuclear membrane. Superresolution microscopy showed that the majority of the AAL signal localizes in proximity to nuclear pore complexes. Host cells modify secreted proteins with O-fucose; here we describe the O-fucosylation pathway in the nucleocytosol of a eukaryote. Furthermore, these results suggest O-fucosylation is a mechanism by which proteins involved in gene expression accumulate near the NPC.

scholarly journals Characterization of a nuclear pore protein sheds light on the roles and composition of the Toxoplasma gondii nuclear pore complex

2017 ◽  
Vol 74 (11) ◽  
pp. 2107-2125 ◽  
Author(s):  
Flavie Courjol ◽  
Thomas Mouveaux ◽  
Kevin Lesage ◽  
Jean-Michel Saliou ◽  
Elisabeth Werkmeister ◽  
...  
Keyword(s):  
Toxoplasma Gondii ◽  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Nuclear Pore Protein ◽  
Pore Protein

Identification and characterisation of structural maintenance of chromosome 1 (smc1) mutants of Coprinopsis cinerea

2008 ◽  
Vol 280 (3) ◽  
Author(s):  
Hajime Muraguchi ◽  
Kousuke Abe ◽  
Minako Nakagawa ◽  
Kiyoto Nakamura ◽  
Sonoe O. Yanagi
Keyword(s):  
Chromosome 1 ◽  
Coprinopsis Cinerea ◽  
Structural Maintenance Of Chromosome

The Formation, Structure, Distribution and Frequency of Nuclear Pores

1971 ◽  
Vol 29 ◽  
pp. 518-519
Author(s):  
G. G. Maul
Keyword(s):  
Nuclear Pore Complex ◽  
Nuclear Membrane ◽  
Dynamic Structure ◽  
Nuclear Pore ◽  
Nuclear Pores ◽  
Filter Function ◽  
Etching Technique ◽  
Selective Filter ◽  
Membranous Part

The chromatin of eukaryotic cells is separated from the cytoplasm by a double membrane. One obvious structural specialization of the nuclear membrane is the presence of pores which have been implicated to facilitate the selective nucleocytoplasmic exchange of a variety of large molecules. Thus, the function of nuclear pores has mainly been regarded to be a passive one. Non-membranous diaphragms, radiating fibers, central rings, and other pore-associated structures were thought to play a role in the selective filter function of the nuclear pore complex. Evidence will be presented that suggests that the nuclear pore is a dynamic structure which is non-randomly distributed and can be formed during interphase, and that a close relationship exists between chromatin and the membranous part of the nuclear pore complex.Octagonality of the nuclear pore complex has been confirmed by a variety of techniques. Using the freeze-etching technique, it was possible to show that the membranous part of the pore complex has an eight-sided outline in human melanoma cells in vitro. Fibers which traverse the pore proper at its corners are continuous and indistinguishable from chromatin at the nucleoplasmic side, as seen in conventionally fixed and sectioned material. Chromatin can be seen in octagonal outline if serial sections are analyzed which are parallel but do not include nuclear membranes (Fig. 1). It is concluded that the shape of the pore rim is due to fibrous material traversing the pore, and may not have any functional significance. In many pores one can recognize a central ring with eight fibers radiating to the corners of the pore rim. Such a structural arrangement is also found to connect eight ribosomes at the nuclear membrane.

Nuclear Envelope Dynamics During Mitosis

1988 ◽  
Vol 46 ◽  
pp. 224-225
Author(s):  
Brian Burke
Keyword(s):  
Nuclear Envelope ◽  
Membrane Vesicles ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Animal Cells ◽  
Interphase Chromosome ◽  
Lamin B ◽  
Chromosome Architecture ◽  
Complex Membrane ◽  
Pore Complexes

The nuclear envelope is a complex membrane structure that forms the boundary of the nuclear compartment in eukaryotes. It regulates the passage of macromolecules between the two compartments and may be important for organizing interphase chromosome architecture. In interphase animal cells it forms a remarkably stable structure consisting of a double membrane ouerlying a protein meshwork or lamina and penetrated by nuclear pore complexes. The latter form the channels for nucleocytoplasmic exchange of macromolecules, At the onset of mitosis, however, it rapidly disassembles, the membranes fragment to yield small vesicles and the lamina, which is composed of predominantly three polypeptides, lamins R, B and C (MW approx. 74, 68 and 65 kDa respectiuely), breaks down. Lamins B and C are dispersed as monomers throughout the mitotic cytoplasm, while lamin B remains associated with the nuclear membrane vesicles.

Structure, assembly and interactions of the nuclear lamina and the nuclear pore complex

1992 ◽  
Vol 50 (1) ◽  
pp. 490-491
Author(s):  
N. Panté ◽  
M. Jarnik ◽  
E. Heitlinger ◽  
U. Aebi
Keyword(s):  
Nuclear Pore Complex ◽  
Divalent Cations ◽  
Nuclear Lamina ◽  
Dynamic Structure ◽  
Nucleocytoplasmic Transport ◽  
Nuclear Pore ◽  
Cytoplasmic Filaments ◽  
Radial Spokes ◽  
Nuclear Ring ◽  
Central Plug

The nuclear pore complex (NPC) is a ∼120 MD supramolecular machine implicated in nucleocytoplasmic transport, that is embedded in the double-membraned nuclear envelope (NE). The basic framework of the ∼120 nm diameter NPC consists of a 32 MD cytoplasmic ring, a 66 MD ‘plug-spoke’ assembly, and a 21 MD nuclear ring. The ‘central plug’ seen in en face views of the NPC reveals a rather variable appearance indicating that it is a dynamic structure. Projecting from the cytoplasmic ring are 8 short, twisted filaments (Fig. 1a), whereas the nuclear ring is topped with a ‘fishtrap’ made of 8 thin filaments that join distally to form a fragile, 30-50 nm distal diameter ring centered above the NPC proper (Fig. 1b). While the cytoplasmic filaments are sensitive to proteases, they as well as the nuclear fishtraps are resistant to RNase treatment. Removal of divalent cations destabilizes the distal rings and thereby opens the fishtraps, addition causes them to reform. Protruding from the tips of the radial spokes into perinuclear space are ‘knobs’ that might represent the large lumenal domain of gp210, a membrane-spanning glycoprotein (Fig. 1c) which, in turn, may play a topogenic role in membrane folding and/or act as a membrane-anchoring site for the NPC. The lectin wheat germ agglutinin (WGA) which is known to recognize the ‘nucleoporins’, a family of glycoproteins having O-linked N-acetyl-glucosamine, is found in two locations on the NPC (Fig. 1. d-f): (i) whereas the cytoplasmic filaments appear unlabelled (Fig. 1d&e), WGA-gold labels sites between the central plug and the cytoplasmic ring (Fig. le; i.e., at a radius of 25-35 nm), and (ii) it decorates the distal ring of the nuclear fishtraps (Fig. 1, d&f; arrowheads).

Pore relations: nuclear pore complexes and nucleocytoplasmic exchange

2000 ◽  
Vol 36 ◽  
pp. 75-88 ◽  
Author(s):  
Michael P. Rout ◽  
John D. Aitchison
Keyword(s):  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Pore Complexes

Vorkommen und Genotypen von Toxoplasma gondii in der Muskulatur von Schaf, Rind und Schwein sowie im Katzenkot in der Schweiz

2012 ◽  
Vol 154 (6) ◽  
pp. 251-255 ◽  
Author(s):  
F. C. Frey ◽  
E. A. Berger-Schoch ◽  
C. D. Herrmann ◽  
G. Schares ◽  
N. Müller ◽  
...  
Keyword(s):  
Toxoplasma Gondii

Altered visual attention behavior of Toxoplasma gondii-infected individuals.

2019 ◽  
Vol 12 (4) ◽  
pp. 485-494
Author(s):  
Joaquim C. Rossini ◽  
Carolina S. Lopes ◽  
Fernanda P. Dirscherl ◽  
Deise A. O. Silva ◽  
José R. Mineo
Keyword(s):  
Toxoplasma Gondii ◽  
Visual Attention
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