Chromatin-Independent Nuclear Envelope Assembly Induced by Ran GTPase in Xenopus Egg Extracts

The nuclear envelope (NE) forms a controlled boundary between the cytoplasm and the nucleus of eukaryotic cells. To facilitate investigation of mechanisms controlling NE assembly, we developed a cell-free system made from Xenopus laevis eggs to study the process in the absence of chromatin. NEs inco...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2000-05, Vol.288 (5470), p.1429-1432
Main Authors: Zhang, Chuanmao, Clarke, Paul R.
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Biological Transport, Active
Cell Cycle Proteins
Cell Extracts
Cell nucleus
Cell structures and functions
Cells
Cellular biology
Chromatin
Chromatin - metabolism
Disease outbreaks
DNA-Binding Proteins - metabolism
Eggs
Fluorescent antibody techniques
Fundamental and applied biological sciences. Psychology
Guanine Nucleotide Exchange Factors
Guanosine Diphosphate - metabolism
Guanosine Triphosphate - metabolism
Imports
Intermediate Filament Proteins
Lamin Type B
Membrane Fusion
Molecular and cellular biology
Molecular biology
Nipah virus
Nuclear Envelope - metabolism
Nuclear Envelope - ultrastructure
nuclear envelopes
Nuclear membrane
Nuclear membranes
Nuclear pore complex proteins
Nuclear Proteins - metabolism
Nucleoplasmins
Ova
Ovum
Phosphoproteins - metabolism
Proteins
ran GTP-Binding Protein - metabolism
Ran protein
Recombinant Fusion Proteins - metabolism
Swine
Telophase
Viruses
Xenopus
Xenopus laevis
Xenopus Proteins
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Description
Summary:The nuclear envelope (NE) forms a controlled boundary between the cytoplasm and the nucleus of eukaryotic cells. To facilitate investigation of mechanisms controlling NE assembly, we developed a cell-free system made from Xenopus laevis eggs to study the process in the absence of chromatin. NEs incorporating nuclear pores were assembled around beads coated with the guanosine triphosphatase Ran, forming pseudo-nuclei that actively imported nuclear proteins. NE assembly required the cycling of guanine nucleotides on Ran and was promoted by RCC1, a nucleotide exchange factor recruited to beads by Ran-guanosine diphosphate (Ran-GDP). Thus, concentration of Ran-GDP followed by generation of Ran-GTP is sufficient to induce NE assembly.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.288.5470.1429