Isolation and fractionation of rat liver nuclear envelopes and nuclear pore complexes

Methods ◽  
2006 ◽  
Vol 39 (4) ◽  
pp. 277-283 ◽  
Author(s):  
Michael J. Matunis
Keyword(s):  
Rat Liver ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Pore Complexes

scholarly journals Rat liver nuclear skeleton and ribonucleoprotein complexes containing HnRNA.

1978 ◽  
Vol 76 (3) ◽  
pp. 675-691 ◽  
Author(s):  
T E Miller ◽  
C Y Huang ◽  
A O Pogo
Keyword(s):  
Rat Liver ◽  
Sulfonyl Chloride ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Morphological Aspect ◽  
Ribonucleoprotein Complexes ◽  
Liver Nuclei ◽  
Rnase Treatment ◽  
Labeled Rna ◽  
Pore Complexes

Rat liver nuclei deprived of chromatin and nucleoplasm show a spongelike network which preserves its connection with nucleoli, the inner membrane of the nuclear envelope, and nuclear pore complexes. It contains all of the HnRNA, provided the endogenous proteolytic activity is inhibited by a proteolytic inhibitor such as phenylmethyl sulfonyl chloride (PMSC) or the fluoride form (PMSF). In the absence of these proteolytic inhibitors, HnRNA is dissociated from the spongelike network and sediments in a sucrose gradient as polydispersed ribonucleoprotein complexes. Furthermore, purified HnRNA as well as rRNA do not bind to the spongelike network when added to these nuclei. These observations demonstrate that the association of HnRNA to the nuclear skeleton is not an artifact. RNase treatment of the spongelike network digests the majority of the rapidly labeled RNA but does not alter the morphological aspect nor the architecture of this network. EDTA and heparin treatments affect neither the attachment of HnRNA nor the structural organization of this network. Electron microscope studies of the network reveal a characteristic flexuous configuration. Its relationship with diffused and condensed chromatin is discussed.

scholarly journals A modified procedure for the isolation of a pore complex-lamina fraction from rat liver nuclei.

1976 ◽  
Vol 70 (3) ◽  
pp. 581-591 ◽  
Author(s):  
N Dwyer ◽  
G Blobel
Keyword(s):  
Nuclear Envelope ◽  
Rat Liver ◽  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Envelope Membrane ◽  
Rat Liver Nuclei ◽  
Liver Nuclei ◽  
Pore Complexes

A modified procedure for the isolation of a nuclear pore complex-lamina fraction from rat liver nuclei is described. Evidence is provided that the isolated lamina, a 150-A thick, proteinaceous structure, apposes the inner nuclear envelope membrane, connecting nuclear pore complexes and surrounding the entire nucleus.

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.

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
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