scholarly journals The Integrity of Nuclear Proteins Following Incubation of Isolated Nuclei in vitro

1975 ◽  
Vol 52 (3) ◽  
pp. 561-566 ◽  
Author(s):  
Susan M. SELLWOOD ◽  
Pamela G. RICHES ◽  
Kenneth R. HARRAP ◽  
David RICKWOOD ◽  
Alexander J. MacGILLIVRAY ◽  
...  
Keyword(s):  
Nuclear Proteins ◽  
Isolated Nuclei

Characterization of a heat shock-induced insoluble complex in the nuclei of cells

1987 ◽  
Vol 88 (1) ◽  
pp. 65-72
Author(s):  
T.D. Littlewood ◽  
D.C. Hancock ◽  
G.I. Evan
Keyword(s):  
Heat Shock ◽  
Nuclear Proteins ◽  
Intact Cells ◽  
Isolated Nuclei ◽  
Insoluble Complex ◽  
Shock Response ◽  
Similar Complex

The formation of an insoluble complex in isolated nuclei incubated at physiological temperature (37 degrees C) is demonstrated. A similar complex is shown to form in the nuclei of intact cells subjected to temperatures that induce the classical heat-shock response. The formation of this complex occurs rapidly in response to hyperthermia and is induced by small increases in temperature both in vitro and in vivo. We have characterized the formation of the complex in isolated nuclei and the nuclei of intact cells. A small number of the subset of nuclear proteins involved in the complex have been identified. The significance of the loss of solubility of these proteins in the nucleus following hyperthermia is discussed.

scholarly journals ADP-ribosylation in isolated nuclei of Physarum polycephalum

1988 ◽  
Vol 253 (3) ◽  
pp. 859-867 ◽  
Author(s):  
G Golderer ◽  
R Schneider ◽  
B Auer ◽  
P Loidl ◽  
P Gröbner
Keyword(s):  
Cell Cycle ◽  
Molecular Mass ◽  
Physarum Polycephalum ◽  
High Mobility ◽  
Nuclear Proteins ◽  
Isolated Nuclei ◽  
Adp Ribosylation ◽  
Adp Ribosyltransferase ◽  
Mass Form

ADP-ribosylation of histones and non-histone nuclear proteins was studied in isolated nuclei during the naturally synchronous cell cycle of Physarum polycephalum. Aside from ADP-ribosyltransferase (ADPRT) itself, histones and high mobility group-like proteins are the main acceptors for ADP-ribose. The majority of these ADP-ribose residues is NH2OH-labile. ADP-ribosylation of the nuclear proteins is periodic during the cell cycle with maximum incorporation in early to mid G2-phase. In activity gels two enzyme forms with Mr of 115,000 and 75,000 can be identified. Both enzyme forms are present at a constant ratio of 3:1 during the cell cycle. The higher molecular mass form cannot be converted in vitro to the low molecular mass form, excluding an artificial degradation during isolation of nuclei. The ADPRT forms were purified and separated by h.p.l.c. The low molecular mass form is inhibited by different ADPRT inhibitors to a stronger extent and is the main acceptor for auto-ADP-ribosylation. The high molecular mass form is only moderately auto-ADP-ribosylated.

In-vivo phytochrome control of in vitro transcription rates in isolated nuclei from oat seedlings

Planta ◽  
1984 ◽  
Vol 161 (5) ◽  
pp. 444-450 ◽  
Author(s):  
Egon M�singer ◽  
Eberhard Sch�fer
Keyword(s):  
In Vitro Transcription ◽  
Isolated Nuclei

scholarly journals Induction and properties of cytoplasmic factor(s) which enhance nuclear nonhistone protein phosphorylation in lymphocytes stimulated by anti-Ig.

1977 ◽  
Vol 146 (3) ◽  
pp. 653-664 ◽  
Author(s):  
Y Nishizawa ◽  
T Kishimoto ◽  
H Kikutani ◽  
Y Yamamura
Keyword(s):  
Protein Kinase ◽  
Protein Phosphorylation ◽  
Adenosine Triphosphate ◽  
Active Substance ◽  
Nuclear Proteins ◽  
Concomitant Increase ◽  
Cytoplasmic Factor ◽  
Nonhistone Protein ◽  
Rabbit Lymphocytes

An increased in vitro phosphorylation of nonhistone nuclear proteins (NHP) was observed in the nuclei isolated from rabbit lymphocytes which had been stimulated with anti-Ig for 4 h. No concomitant increase of phosphorylation in histones or 0.14 M NaCl-soluble proteins was observed. The increase of in vitro phosphorylation of NHP was also observed in the nuclei isolated from nonstimulated cells when these nuclei were preincubated for 2 h with cell-free extracts from anti-Ig-stimulated cells. The active substance in cell-free extracts was maximally induced when lymphocytes were stimulated with anti-Ig for 2 h. The induction of an increased phosphorylation of NHP in nonstimulated nuclei with the cell-free extracts was not due to decrease of the adenosine triphosphate pool in the extracts from anti-Ig-stimulated cells. The active substance in cell-free extracts was not NHP-protein kinase itself, but it probably activated NHP-protein kinase in quiescent nuclei. The active substance was nondialyzable and probably protein. It was resistant against heating at 56 degrees C for 30 min, but the activity was completely destroyed by heating at 90 degrees C for 30 min. The active substance may be responsible for the transduction of the membrane-mediated signals given through Ig receptors to nuclei.

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