Studies on the interaction of the human c-myc protein with cell nuclei: p62c-myc as a member of a discrete subset of nuclear proteins

Cell ◽  
1985 ◽  
Vol 43 (1) ◽  
pp. 253-261 ◽  
Author(s):  
G Evan
Keyword(s):  
Nuclear Proteins ◽  
Discrete Subset ◽  
Cell Nuclei

scholarly journals Histone carbonylation in vivo and in vitro

2000 ◽  
Vol 351 (3) ◽  
pp. 769-777 ◽  
Author(s):  
Georg T. WONDRAK ◽  
Daniel CERVANTES-LAUREAN ◽  
Elaine L. JACOBSON ◽  
Myron K. JACOBSON
Keyword(s):  
Histone H1 ◽  
Nuclear Proteins ◽  
Carbonyl Groups ◽  
Cell Nuclei ◽  
Strand Breaks ◽  
Core Histones ◽  
Dna Strand ◽  
And Function

Non-enzymic damage to nuclear proteins has potentially severe consequences for the maintenance of genomic integrity. Introduction of carbonyl groups into histones in vivo and in vitro was assessed by Western blot immunoassay and reductive incorporation of tritium from radiolabelled NaBH4 (sodium borohydride). Histone H1 extracted from bovine thymus, liver and spleen was found to contain significantly elevated amounts of protein-bound carbonyl groups as compared with core histones. The carbonyl content of nuclear proteins of rat pheochromocytoma cells (PC12 cells) was not greatly increased following oxidative stress induced by H2O2, but was significantly increased following alkylating stress induced by N-methyl-N´-nitro-N-nitrosoguanidine or by combined oxidative and alkylating stress. Free ADP-ribose, a reducing sugar generated in the nucleus in proportion to DNA strand breaks, was shown to be a potent histone H1 carbonylating agent in isolated PC12 cell nuclei. Studies of the mechanism of histone H1 modification by ADP-ribose indicate that carbonylation involves formation of a stable acyclic ketoamine. Our results demonstrate preferential histone H1 carbonylation in vivo, with potentially important consequences for chromatin structure and function.

Differential accumulation of oocyte nuclear proteins by embryonic nuclei of Xenopus

Development ◽  
1987 ◽  
Vol 101 (4) ◽  
pp. 829-846 ◽  
Author(s):  
C. Dreyer
Keyword(s):  
De Novo ◽  
Germinal Vesicle ◽  
Intrinsic Property ◽  
Nuclear Proteins ◽  
Cell Nuclei ◽  
Germinal Vesicle Breakdown ◽  
Early Stages ◽  
Nuclear Antigens ◽  
Gradual Process ◽  
Oocyte Nuclear Proteins

Oocyte nuclear proteins of Xenopus are distributed into the cytoplasm of the maturing egg after germinal vesicle breakdown. Later they are found in all cell nuclei of the embryo. At early stages of development, different nuclear proteins behave differently. A class of ‘early shifting’ antigens is accumulated by pronuclei and cleavage nuclei, whereas others appear to be excluded from the nuclei at early stages but are shifted into the nuclei at blastula or during and after gastrulation. Accumulation of ‘late-shifting’ nuclear antigens is a gradual process and occurs during a period characteristic of each protein. Multiple artificial pronuclei can be formed after injection of sperm nuclei, erythrocyte nuclei or pure lambda-DNA into unfertilized eggs. The artificial pronuclei accumulate early- but not late-shifting proteins. Early-migrating proteins rapidly accumulate into the germinal vesicle after de novo synthesis in the oocyte, indicating that the efficiency of translocation into nuclei is an intrinsic property of each protein. Artificial extension of the length of the cell cycle before midblastula transition does not lead to accumulation of the late-shifting nuclear antigens investigated.

scholarly journals Changes in non-histone nuclear proteins during postnatal myocardial development

1983 ◽  
Vol 210 (1) ◽  
pp. 175-182
Author(s):  
G Jackowski ◽  
C C Liew
Keyword(s):  
Myocardial Cell ◽  
Nuclear Proteins ◽  
Synthetic Activity ◽  
Cell Nuclei ◽  
Progressive Loss ◽  
Myocardial Development ◽  
Group A ◽  
Specific Proteins ◽  
Group B

Myocardial-cell nuclei isolated from ventricles of rats between 4 days and 15 months of age showed a progressive loss of DNA-synthetic activity in vitro. Correlated with this loss is the differential appearance of three major groups of non-histone nuclear proteins. Group a, with pI5.7-6.5 and Mr 67000, appeared in detectable amounts in rats more than 10 days of age, whereas group b, consisting of proteins with pI6.8-7.2 and Mr 45000, appeared in rats older than 33 days. The third group (group c), with pI6.5-8.5 and Mr 32000-42000, was present throughout postnatal development, but the amount of these proteins appeared to be greater in the 10-day-old rat than in the 15-month-old rat. All groups of these specific proteins were localized within the nucleus and did not reflect cytoplasmic constituents. Furthermore, the amino acid compositions of these polypeptides were also analysed and compared with those of actin and tubulin.

scholarly journals ANTIGEN-INDUCED CHANGES IN LYMPHOID CELL HISTONES

1965 ◽  
Vol 26 (1) ◽  
pp. 201-208 ◽  
Author(s):  
Maurice M. Black ◽  
Hudson R. Ansley
Keyword(s):  
Dna Content ◽  
Renal Cell ◽  
Acute Effect ◽  
Nuclear Proteins ◽  
Renal Cells ◽  
Cell Nuclei ◽  
Feulgen Staining ◽  
Fast Green ◽  
Induced Changes ◽  
Ammoniacal Silver

An acute effect of antigens on the nuclear histones of mouse thymocytes was investigated by means of cytophotometric measurements of thymocytes stained with ammoniacal-silver (A-S) and with fast green (FG). In addition, the DNA content was measured in terms of Feulgen staining. In terms of such staining it appeared that nuclei of control thymocytes contain a greater amount of nuclear histones and a higher histone/DNA ratio than do renal cell nuclei from the same animal. Within 1 hour after the injection of antigen the thymocyte nuclei appear to lose approximately 32 per cent and 20 per cent, respectively, of A-S and FG stainable nuclear proteins, while the Feulgen staining remains unchanged. Since the renal cell nuclei show no antigen-induced change in histone staining, the histone staining and histone/DNA ratios were found to be similar in the thymocytes and renal cells of the antigen-injected mice. The antigen-induced loss of thymocyte histones was also found to be associated with a change in the color of the A-S staining, from yellowish brown to black. This and other findings suggest that thymocyte nuclei contain an antigen-labile, lysine-rich histone. The implication of these observations in regard to the phenomenon of immunological competence is discussed and the need for continued investigation indicated.

scholarly journals Poly(adenosine diphosphate ribose) synthetase activity in nuclei of dividing and of non-dividing but differentiating intestinal epithelial cells

1979 ◽  
Vol 180 (3) ◽  
pp. 455-461 ◽  
Author(s):  
J W Porteous ◽  
H M Furneaux ◽  
C K Pearson ◽  
C M Lake ◽  
A Morrison
Keyword(s):  
Small Intestine ◽  
Epithelial Cells ◽  
Guinea Pig ◽  
Intestinal Epithelial Cells ◽  
Adenosine Diphosphate ◽  
Crypt Cell ◽  
Nuclear Proteins ◽  
Synthetase Activity ◽  
Intestinal Epithelial ◽  
Cell Nuclei

Poly(ADP-ribose) synthetase activity is found in nuclei of regenerating epithelial cells in the lower half of the crypts of guinea-pig small intestine. Nuclei from non-dividing but differentiating and maturing cells in the upper crypts and on the villi contain no more than about 10% of the synthetase activity of lower-crypt cell nuclei. The product in the active nuclei is shown to be 80% poly(ADP-ribosylated) protein and 20% mono(ADP-ribosylated) protein; 60% of thetotal labelled product was attached to acid-soluble proteins (including histones), and 40% to acid-insoluble (non-histone) proteins. The average number of ADP-ribosyl units in the oligomeric chains of the poly(ADP-ribosylated) proteins was 15 but the range of sizes of (ADP-ribose) oligomers attached to nuclear proteins was smaller in villus than in crypt cell nuclei.

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