Photoaffinity labeling of the major nucleoside triphosphatase of rat liver nuclear envelope

Biochemistry ◽  
1984 ◽  
Vol 23 (15) ◽  
pp. 3501-3507 ◽  
Author(s):  
Gary A. Clawson ◽  
C. H. Woo ◽  
Jane Button ◽  
Edward A. Smuckler
Keyword(s):  
Nuclear Envelope ◽  
Rat Liver ◽  
Photoaffinity Labeling ◽  
Nucleoside Triphosphatase

Considerations in the isolation of rat liver nuclear matrix, nuclear envelope, and pore complex lamina

1981 ◽  
Vol 132 (1) ◽  
pp. 105-123 ◽  
Author(s):  
Scott H. Kaufmann ◽  
Donald S. Coffey ◽  
Joel H. Shaper
Keyword(s):  
Nuclear Envelope ◽  
Rat Liver ◽  
Nuclear Matrix

scholarly journals Ribonucleic acid stimulation of mammalian liver nuclear-envelope nucleoside triphosphatase. A possible enzymic marker for the nuclear envelope

1977 ◽  
Vol 162 (3) ◽  
pp. 671-679 ◽  
Author(s):  
P S Agutter ◽  
J R Harris ◽  
I Stevenson
Keyword(s):  
Nuclear Envelope ◽  
Specific Activity ◽  
Assay Medium ◽  
Exogenous Rna ◽  
Mammalian Liver ◽  
High Concentrations ◽  
Enzymic Marker ◽  
Stimulation Of ◽  
Nucleoside Triphosphatase

1. The specific activity of rat and pig liver nuclear-envelope nucleoside triphosphatase (EC 3.6.1.3) decreases when the system is depleted of RNA. The activity can be restored by adding high concentrations of yeast RNA to the assay medium. 2. Exogenous RNA also increases the activity of the enzyme in control envelopes (not RNA-depleted). The effect appears to be largely specific for poly(A) and poly(G); it is not stimulated by rRNA or tRNA preparations, ribonuclease-hydrolysed RNA, AMP, or double- or single-stranded DNA. 3. Inhibitors of the enzyme, in concentrations at which half-maximal inhibition of the enzyme is achieved, do not affect the percentage stimulation of the enzyme by yeast RNA. 4. The simulation is abolished by the inclusion of 150 mM-KCl or -NaCl in the assay medium, but not by increasing the assay pH to 8.5. 5. The results are discussed in the light of the possible role of the nucleoside triphosphatase in vivo in nucleo-cytoplasmic ribonucleoprotein translocation. 6. It is proposed that poly(G)-stimulated Mg2+-activated adenosine triphosphatase activity should be adopted as an enzymic marker for the nuclear envelope.

scholarly journals Cytochemical studies on the relation of nucleoside triphosphatase activity to ribonucleoproteins in isolated rat liver nuclei.

1980 ◽  
Vol 28 (1) ◽  
pp. 27-35 ◽  
Author(s):  
A Vorbrodt ◽  
G G Maul
Keyword(s):  
Nuclear Envelope ◽  
Rat Liver ◽  
Enzyme Reaction ◽  
Point Of View ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Isolated Rat Liver ◽  
Rat Liver Nuclei ◽  
Liver Nuclei ◽  
Isolated Rat

Cytochemical tests for nucleosidetriphosphatase (NTPase) and Bernhard's preferential staining for ribonucleoproteins (RNP) were applied to isolated rat liver nuclei. The strongest and most easily reproducible positive reaction for NTPase was detected at pH 7.7 with ATP and GTP. This reaction was activated by Mg2+ and Ca2+ and inhibited by Be2+, Zn2+, quercetin, and ribonuclease. The major sites of enzyme reaction were intranuclear RNA-containing structures. Incubation of nuclei in ATP-stimulated RNA-release medium eliminated a considerable part of the material showing both NTPase reaction and staining for RNP; the perichromatin granules disappeared, while interchromatin granules remained. NTPase activity in the nuclear envelope seems to be associated with the annular part of nuclear pore complexes (permanent component) and with RNP particles translocated through nuclear pores or attached to the surface of nuclei (transitional component). From a morphological point of view, these observations support previous biochemical data suggesting the existence of a connection between NTPase activity and the translocation of RNP particles through the nuclear envelope.

The role of protein phosphokinase and protein phosphatase during the nuclear envelope nucleoside triphosphatase reaction

1984 ◽  
Vol 773 (2) ◽  
pp. 308-316 ◽  
Author(s):  
Michael Bachmann ◽  
August Bernd ◽  
Heinz C. Schröder ◽  
Rudolf K. Zahn ◽  
Werner E.G. Müller
Keyword(s):  
Nuclear Envelope ◽  
Protein Phosphatase ◽  
Nucleoside Triphosphatase

scholarly journals cAMP-dependent protein kinase phosphorylates and activates nuclear Ca2+-ATPase

1998 ◽  
Vol 95 (16) ◽  
pp. 9178-9183 ◽  
Author(s):  
Patrick J. Rogue ◽  
Jean-Paul Humbert ◽  
Alphonse Meyer ◽  
Solange Freyermuth ◽  
Marie-Marthe Krady ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Nuclear Envelope ◽  
Rat Liver ◽  
Protein Band ◽  
Partial Purification ◽  
Dependent Protein Kinase ◽  
Rat Liver Nuclei ◽  
Camp Dependent Protein Kinase ◽  
Dependent Protein ◽  
Liver Nuclei

A Ca2+-pump ATPase, similar to that in the endoplasmic reticulum, has been located on the outer membrane of rat liver nuclei. The effect of cAMP-dependent protein kinase (PKA) on nuclear Ca2+-ATPase (NCA) was studied by using purified rat liver nuclei. Treatment of isolated nuclei with the catalytic unit of PKA resulted in the phosphorylation of a 105-kDa band that was recognized by antibodies specific for sarcoplasmic reticulum Ca2+-ATPase type 2b. Partial purification and immunoblotting confirmed that the 105-kDa protein band phosphorylated by PKA is NCA. The stoichiometry of phosphorylation was 0.76 mol of phosphate incorporated/mol of partially purified enzyme. Measurement of ATP-dependent 45Ca2+ uptake into purified nuclei showed that PKA phosphorylation enhanced the Ca2+-pumping activity of NCA. We show that PKA phosphorylation of Ca2+-ATPase enhances the transport of 10-kDa fluorescent-labeled dextrans across the nuclear envelope. The findings reported in this paper are consistent with the notion that the crosstalk between the cAMP/PKA- and Ca2+-dependent signaling pathways identified at the cytoplasmic level extends to the nucleus. Furthermore, these data support a function for crosstalk in the regulation of calcium-dependent transport across the nuclear envelope.

scholarly journals Proteins from rat liver cytosol which stimulate mRNA transport. Purification and interactions with the nuclear envelope mRNA translocation system

1986 ◽  
Vol 159 (1) ◽  
pp. 51-59 ◽  
Author(s):  
Heinz C. SCHRODER ◽  
Michael ROTTMANN ◽  
Michael BACHMANN ◽  
Werner E. G. MULLER ◽  
Alexander R. McDONALD ◽  
...  
Keyword(s):  
Nuclear Envelope ◽  
Rat Liver ◽  
Mrna Transport ◽  
Liver Cytosol ◽  
Rat Liver Cytosol
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