In vitro transfer of N,N′-diacetylchitobiose to glycoproteins in rat liver nuclei

1992 ◽  
Vol 70 (8) ◽  
pp. 677-683 ◽  
Author(s):  
Jacques Frot—Coutaz ◽  
Agnès Degiuli ◽  
Marie-Bénédicte Martel ◽  
Robert Létoublon
Keyword(s):  
Rat Liver ◽  
Biological Significance ◽  
Nuclear Proteins ◽  
Direct Transfer ◽  
Rat Liver Nuclei ◽  
Liver Nuclei

This work demonstrates that (N-acetyl[14C]glucosamine)2 is transferred from dolichyl pyrophosphate – (N-acetyl[14C]glucosamine)2 to endogenous nuclear glycoproteins. The (N-acetyl[l4C]gIucosamine)2 moiety is N-linked, since it can be released from the tryptic glycopeptides by N-glycosidase F and by hydrazinolysis, but not by β-elimination. The biological significance of this direct transfer of N, N′-diacetylchitobiose to nuclear proteins remains to be elucidated.Key words: nucleus, nuclear glycoproteins, nuclear N-acetylglucosaminyltransferase, N,N′ -diacetylchitobiose.

scholarly journals Nuclear-envelope vesicles as a model system to study nucleocytoplasmic transport. Specific uptake of nuclear proteins

1987 ◽  
Vol 241 (1) ◽  
pp. 213-219 ◽  
Author(s):  
N Riedel ◽  
H Fasold
Keyword(s):  
Nuclear Envelope ◽  
Rat Liver ◽  
Protein Translocation ◽  
High Mobility ◽  
Preceding Paper ◽  
Nucleocytoplasmic Transport ◽  
Nuclear Proteins ◽  
Rat Liver Nuclei ◽  
Liver Nuclei

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.

scholarly journals Modulation by Exogenous Histones of Phosphorylation of Non-Histone Nuclear Proteins in Isolated Rat Liver Nuclei

1973 ◽  
Vol 248 (21) ◽  
pp. 7595-7600
Author(s):  
Edward M. Johnson ◽  
Giorgio Vidali ◽  
Virginia C. Littau ◽  
Vincent G. Allfrey
Keyword(s):  
Rat Liver ◽  
Nuclear Proteins ◽  
Isolated Rat Liver ◽  
Rat Liver Nuclei ◽  
Liver Nuclei ◽  
Isolated Rat
Sign in / Sign up

Export Citation Format

Share Document