Response of isolated nuclei to phospholipid vesicles: Analysis of the nuclear proteins after treatment with phosphatidylserine and phosphatidylcholine and comparison with heparin

1984 ◽  
Vol 8 (4) ◽  
pp. 289-296 ◽  
Author(s):  
S CAPITANI ◽  
L COCCO ◽  
A MATTEUCCI ◽  
E CARAMELLI ◽  
S PAPA ◽  
...  
Keyword(s):  
Nuclear Proteins ◽  
Phospholipid Vesicles ◽  
Isolated Nuclei

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

scholarly journals Influence of histones and calcium and magnesium ions on the ultrastructure of chromatin in isolated nuclei of Pinus silvestris L. root meristem

2015 ◽  
Vol 45 (1–2) ◽  
pp. 45-57
Author(s):  
Halina Michniewicz
Keyword(s):  
Root Meristem ◽  
The Other ◽  
Nuclear Proteins ◽  
Magnesium Ions ◽  
Pinus Silvestris ◽  
Control Material ◽  
Isolated Nuclei ◽  
Calcium And Magnesium ◽  
Calcium And Magnesium Ions

The width of chromatin fibrils in nuclei fixed in situ is about 10 nm. In nuclei isolated in the presence of Ca<sup>+2</sup> and Mg<sup>+2</sup> ions the fibrils coalesce, and thus their width secondarily increases, whereas in nuclei isolated without the presence of the cations the diameter of fibrils increases somewhat as compared with that in nuclei in situ, probably owing to absorption of nonchromatin nuclear proteins. Lysine histone extraction caused dispersion of condensed chromatin, and reintroduction of these proteins - its reconstruction. On the other hand, extraction and reintroduction of the arginine histone did not cause chromatin dispersion, but rather coalescence of the chromatin mass. Lysine histone extraction from material isolated in the presence of Ca<sup>+2</sup> and Mg<sup>+2</sup> ions caused the appearance of a large number of 10-nm fibrils, only sporadically seen in the control material, and disappearance of the 30-nm forms. Reintroduction of the lysine histone reduced the number of single fibrils and enhanced the appearance of coalescent form with 30 nm diameter. Removal of arginine histones did not produce disappearance of single fibrils, but reduced their diameter. Reintroduction of this fraction caused coalescence of chromatin threads, owing to which 90 per cent of the population consisted of fibrils with diameter around 30 nm.

Response of isolated nuclei to phospholipid vesicles: Effect of phosphatidylserine on alpha and beta DNA polymerase activity

1987 ◽  
Vol 11 (5) ◽  
pp. 397-403 ◽  
Author(s):  
L COCCO ◽  
S MISCIA ◽  
A CATALDI ◽  
S CAPITANI ◽  
A MATTEUCCI ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Polymerase Activity ◽  
Phospholipid Vesicles ◽  
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.

Protamine-DNA interaction

1978 ◽  
Vol 36 (2) ◽  
pp. 200-201
Author(s):  
D.P. Bazett-Jones ◽  
F.P. Ottensmeyer
Keyword(s):  
Small Volume ◽  
Double Helix ◽  
Dna Interaction ◽  
Dark Field ◽  
Sperm Head ◽  
Nuclear Proteins ◽  
Field Electron Microscopy ◽  
Dark Field Electron ◽  
Dna Double Helix ◽  
Positively Charged

Dark field electron microscopy has been used for the study of the structure of individual macromolecules with a resolution to at least the 5Å level. The use of this technique has been extended to the investigation of structure of interacting molecules, particularly the interaction between DNA and fish protamine, a class of basic nuclear proteins of molecular weight 4,000 daltons.Protamine, which is synthesized during spermatogenesis, binds to chromatin, displaces the somatic histones and wraps up the DNA to fit into the small volume of the sperm head. It has been proposed that protamine, existing as an extended polypeptide, winds around the minor groove of the DNA double helix, with protamine's positively-charged arginines lining up with the negatively-charged phosphates of DNA. However, viewing protamine as an extended protein is inconsistent with the results obtained in our laboratory.

A heteronuclear and homonuclear filtering strategy for studying the structure of membrane peptides in non-deuterated phospholipid vesicles

1998 ◽  
Vol 95 (2) ◽  
pp. 221-224
Author(s):  
B. T. Doan ◽  
C. Nezry ◽  
L. Rene ◽  
B. Badet ◽  
J. C. Beloeil
Keyword(s):  
Phospholipid Vesicles ◽  
Membrane Peptides
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