ArticleThe Biochemical journal1987
Nuclear-envelope vesicles as a model system to study nucleocytoplasmic transport. Specific uptake of nuclear proteins.
Article in The Biochemical journal, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 23 citations in OpenAlex.
- Temporal association of the herpes simplex virus genome with histone proteins during a lytic infection.Journal of virology · 2008Article
- A novel function for the 90 kDa heat-shock protein (Hsp90): facilitating nuclear export of 60 S ribosomal subunits.The Biochemical journal · 2002Article
- Association with capsid proteins promotes nuclear targeting of simian virus 40 DNA.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Histone-poly(A) hybrid molecules as tools to block nuclear pores.Journal of protein chemistry · 1995Article
- GTP-binding proteins in rat liver nuclear envelopes.Proceedings of the National Academy of Sciences of the United States of America · 1990Article
- Signal-dependent translocation of simian virus 40 large-T antigen into rat liver nuclei in a cell-free system.Molecular and cellular biology · 1987Article
- Permeability measurements with closed vesicles from rat liver nuclear envelopes.Proceedings of the National Academy of Sciences of the United States of America · 1987Article
- Preparation and characterization of nuclear-envelope vesicles from rat liver nuclei.The Biochemical journal · 1987Article
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Authors and funding
2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
In the preceding paper [Riedel & Fasold (1987) Biochem. J. 241, 203-212] we have described a procedure for the preparation of nuclear-envelope vesicles (NE vesicles) from rat liver nuclei. These vesicles, which are largely free of components of the nuclear interior, were employed in an assay system in vitro to study protein translocation across the NE. We found that nuclear proteins such as histones, high-mobility-group proteins and acidic chromosomal proteins are specifically taken up and accumulated in the NE vesicles, whereas there is little or no affinity for non-nuclear proteins like immunoglobulin, myoglobin and cytochrome c. The kinetics of histone uptake into the NE vesicles are similar to those obtained for whole rat liver nuclei, and comparative studies with non-vesicular NEs prepared by deoxyribonuclease I-treatment (DNAase-NEs) indicate that the NE of the vesicles affects the uptake kinetics and increases the capacity for nuclear proteins. The uptake of histones into NE vesicles, but not the binding to DNAase-NEs, can be stimulated by GTP and GDP. Furthermore, we found that even very large molecules can be entrapped in the vesicles during their preparation. These results indicate that the NE vesicles might provide a useful system in vitro with which to investigate the structures and mechanisms involved in protein translocation across the NE.
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