Exploring Nuclear Pore Complex Molecular Architecture by Immuno-Electron Microscopy Using Xenopus Oocytes

2014 ◽  
pp. 81-98 ◽  
Author(s):  
Nelly Panté ◽  
Birthe Fahrenkrog
Keyword(s):  
Electron Microscopy ◽  
Nuclear Pore Complex ◽  
Xenopus Oocytes ◽  
Nuclear Pore ◽  
Molecular Architecture ◽  
Immuno Electron Microscopy

scholarly journals A large particle associated with the perimeter of the nuclear pore complex.

1982 ◽  
Vol 93 (1) ◽  
pp. 63-75 ◽  
Author(s):  
P N Unwin ◽  
R A Milligan
Keyword(s):  
Electron Microscopy ◽  
Nuclear Pore Complex ◽  
Large Particle ◽  
Xenopus Oocytes ◽  
Three Dimensional ◽  
Central Axis ◽  
Dimensional Structure ◽  
Nuclear Pore ◽  
Three Dimensional Structure ◽  
Large Particles

The three-dimensional structure of the nuclear pore complex has been determined to a resolution of approximately 90 A by electron microscopy using nuclear envelopes from Xenopus oocytes. It is shown to be an assembly of several discrete constituents arranged with octagonal symmetry about a central axis. There are apparent twofold axes perpendicular to the octad axis which suggest that the framework of the pore complex is constructed from two equal but oppositely facing halves. The half facing the cytoplasm is in some instances decorated by large particles, similar in appearance and size to ribosomes.

Molecular architecture of the inner ring scaffold of the human nuclear pore complex

Science ◽  
2016 ◽  
Vol 352 (6283) ◽  
pp. 363-365 ◽  
Author(s):  
J. Kosinski ◽  
S. Mosalaganti ◽  
A. von Appen ◽  
R. Teimer ◽  
A. L. DiGuilio ◽  
...  
Keyword(s):  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Molecular Architecture

scholarly journals Isolation of the yeast nuclear pore complex.

1993 ◽  
Vol 123 (4) ◽  
pp. 771-783 ◽  
Author(s):  
M P Rout ◽  
G Blobel
Keyword(s):  
Electron Microscopy ◽  
Image Reconstruction ◽  
Nuclear Pore Complex ◽  
Sedimentation Coefficient ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Negative Stain ◽  
Negative Stain Electron Microscopy ◽  
Pore Complexes

Nuclear pore complexes (NPCs) have been isolated from the yeast Saccharomyces. Negative stain electron microscopy of the isolated NPCs and subsequent image reconstruction revealed the octagonal symmetry and many of the ultrastructural features characteristic of vertebrate NPCs. The overall dimensions of the yeast NPC, both in its isolated form as well as in situ, are smaller than its vertebrate counterpart. However, the diameter of the central structures are similar. The isolated yeast NPC has a sedimentation coefficient of approximately 310 S and an M(r) of approximately 66 MD. It retains all but one of the eight known NPC proteins. In addition it contains as many as 80 uncharacterized proteins that are candidate NPC proteins.

scholarly journals The Yeast Nuclear Pore Complex

2000 ◽  
Vol 148 (4) ◽  
pp. 635-652 ◽  
Author(s):  
Michael P. Rout ◽  
John D. Aitchison ◽  
Adisetyantari Suprapto ◽  
Kelly Hjertaas ◽  
Yingming Zhao ◽  
...  
Keyword(s):  
Nuclear Pore Complex ◽  
Nucleocytoplasmic Transport ◽  
Comprehensive Approach ◽  
Nuclear Pore ◽  
Molecular Architecture ◽  
Gating Mechanism ◽  
Molecular Components

An understanding of how the nuclear pore complex (NPC) mediates nucleocytoplasmic exchange requires a comprehensive inventory of the molecular components of the NPC and a knowledge of how each component contributes to the overall structure of this large molecular translocation machine. Therefore, we have taken a comprehensive approach to classify all components of the yeast NPC (nucleoporins). This involved identifying all the proteins present in a highly enriched NPC fraction, determining which of these proteins were nucleoporins, and localizing each nucleoporin within the NPC. Using these data, we present a map of the molecular architecture of the yeast NPC and provide evidence for a Brownian affinity gating mechanism for nucleocytoplasmic transport.

scholarly journals Correlative super-resolution fluorescence and electron microscopy of the nuclear pore complex with molecular resolution

2014 ◽  
Vol 127 (20) ◽  
pp. 4351-4355 ◽  
Author(s):  
Anna Löschberger ◽  
Christian Franke ◽  
Georg Krohne ◽  
Sebastian van de Linde ◽  
Markus Sauer
Keyword(s):  
Electron Microscopy ◽  
Nuclear Pore Complex ◽  
Super Resolution ◽  
Nuclear Pore ◽  
Fluorescence And Electron Microscopy

scholarly journals The role of the integral membrane nucleoporins Ndc1p and Pom152p in nuclear pore complex assembly and function

2006 ◽  
Vol 173 (3) ◽  
pp. 361-371 ◽  
Author(s):  
Alexis S. Madrid ◽  
Joel Mancuso ◽  
W. Zacheus Cande ◽  
Karsten Weis
Keyword(s):  
Electron Microscopy ◽  
Saccharomyces Cerevisiae ◽  
Nuclear Envelope ◽  
Lipid Bilayers ◽  
Nuclear Pore Complex ◽  
Transmembrane Proteins ◽  
Nuclear Pore ◽  
Large Channel ◽  
And Function

The nuclear pore complex (NPC) is a large channel that spans the two lipid bilayers of the nuclear envelope and mediates transport events between the cytoplasm and the nucleus. Only a few NPC components are transmembrane proteins, and the role of these proteins in NPC function and assembly remains poorly understood. We investigate the function of the three integral membrane nucleoporins, which are Ndc1p, Pom152p, and Pom34p, in NPC assembly and transport in Saccharomyces cerevisiae. We find that Ndc1p is important for the correct localization of nuclear transport cargoes and of components of the NPC. However, the role of Ndc1p in NPC assembly is partially redundant with Pom152p, as cells lacking both of these proteins show enhanced NPC disruption. Electron microscopy studies reveal that the absence of Ndc1p and Pom152p results in aberrant pores that have enlarged diameters and lack proteinaceous material, leading to an increased diffusion between the cytoplasm and the nucleus.

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