Physical properties of DNA and chromatin isolated from G1- and S-phase HeLa S-3 cells. Effects of histone H1 phosphorylation and stage-specific nonhistone chromosomal proteins on the molar ellipticity of native and reconstituted nucleoproteins during thermal denaturation

Biochemistry ◽  
1979 ◽  
Vol 18 (7) ◽  
pp. 1333-1344 ◽  
Author(s):  
Thomas W. Dolby ◽  
Kozo Ajiro ◽  
Thaddeus W. Borun ◽  
R. Stewart Gilmour ◽  
Alfred Zweidler ◽  
...  
Keyword(s):  
Physical Properties ◽  
Thermal Denaturation ◽  
Histone H1 ◽  
S Phase ◽  
Chromosomal Proteins ◽  
Molar Ellipticity

Distinct effects of histone H1 and non-histone chromosomal proteins on the structure of nucleosomes and the chromatin fibre in solution

1985 ◽  
Vol 7 (2) ◽  
pp. 122-124 ◽  
Author(s):  
Stephan I. Dimitrov ◽  
Vladimir L. Makarov ◽  
Lyuben N. Marekov ◽  
Beltcho G. Beltchev
Keyword(s):  
Histone H1 ◽  
Chromosomal Proteins ◽  
Chromatin Fibre

scholarly journals Histone H1 interphase phosphorylation becomes largely established in G1 or early S phase and differs in G1 between T-lymphoblastoid cells and normal T cells

2011 ◽  
Vol 4 (1) ◽  
pp. 15 ◽  
Author(s):  
Anna Gréen ◽  
Bettina Sarg ◽  
Henrik Gréen ◽  
Anita Lönn ◽  
Herbert H Lindner ◽  
...  
Keyword(s):  
T Cells ◽  
Histone H1 ◽  
S Phase ◽  
Lymphoblastoid Cells

scholarly journals CHROMATIN STRUCTURE AND THE CELL DIVISION CYCLE

1972 ◽  
Vol 55 (2) ◽  
pp. 322-327 ◽  
Author(s):  
Thoru Pederson ◽  
Elliott Robbins
Keyword(s):  
Nuclear Dna ◽  
Binding Capacity ◽  
Nuclear Dna Content ◽  
Living Cells ◽  
S Phase ◽  
Minimal Level ◽  
Binding Profile ◽  
Chromosomal Proteins ◽  
Isolated Nuclei ◽  
Degree Of Association

Measurements of actinomycin-3H binding in synchronized HeLa cells reveal that the binding capacity of chromatin decreases progressively during the S phase despite a doubling of nuclear DNA content, reaches a minimal level during G2 and mitosis, and then increases gradually throughout the subsequent G1 interval. Since this pattern was evident in experiments with living cells, ethanol-fixed cells, and isolated nuclei, but not with purified DNA, the actinomycin binding profile may reflect changes in the degree of association between DNA and chromosomal proteins at different stages of the cell cycle.

scholarly journals Non-histone chromosomal proteins. Evidence for their role in mediating the binding of histones to deoxyribonucleic acid during the cell cycle

1974 ◽  
Vol 139 (1) ◽  
pp. 71-76 ◽  
Author(s):  
Gary S. Stein ◽  
Gale Hunter ◽  
Lena Lavie
Keyword(s):  
Cell Cycle ◽  
Deoxyribonucleic Acid ◽  
Sodium Deoxycholate ◽  
S Phase ◽  
Template Activity ◽  
Chromosomal Proteins ◽  
Ionic Detergent ◽  
Selective Dissociation ◽  
Chromatin Template ◽  
Mitotic Cells

By selective dissociation of histones with the ionic detergent sodium deoxycholate, we have demonstrated that these basic chromosomal polypeptides, which are effective inhibitors of transcription, are more tenaciously bound to DNA in mitotic than in S-phase chromatin. Evidence is presented which suggests that cell-cycle-stage-specific non-histone chromosomal proteins can account for such variations in the association of histones with DNA. When chromatin is reconstituted with DNA and histones are pooled from S-phase and mitotic cells and either S-phase or mitotic non-histone chromosomal proteins, a preferential extraction of histones with sodium deoxycholate from chromatin reconstituted with S-phase rather than mitotic non-histone chromosomal proteins is observed. In contrast, the extractability of histones with sodium deoxycholate from nucleohistone complexes reconstituted with DNA pooled from S-phase and mitotic cells and either S-phase or mitotic histones is identical. Since non-histone chromosomal proteins rather than histones are responsible for the differences in chromatin template activity during S-phase and mitosis, we propose that non-histone chromosomal proteins may modify gene expression during the cell cycle by mediating the binding of histones to DNA.

scholarly journals Asynchronous appearance of newly synthesized histone H1 subfractions in HeLa chromatin.

1981 ◽  
Vol 90 (2) ◽  
pp. 415-417 ◽  
Author(s):  
S R Sizemore ◽  
R D Cole
Keyword(s):  
Hela Cells ◽  
Histone H1 ◽  
S Phase ◽  
H1 Histone ◽  
Chromatographic Peaks

Incorporation of radioactive alanine into chromatin-bound subfractions of H1 histone was studied in HeLa cells synchronized by the double thymidine block technique. The subfractions were resolved into three chromatographic peaks by Biorex-70. In the period 5-7 h after release from the thymidine block, peaks I and III showed twice as much incorporation as they did in the period 1-3 h after release, whereas peak II showed three times the incorporation at 5-7 h that it did at 1-3 h. Thus, the H1-histone subfraction in peak II appears in chromatin somewhat later in S phase than do the subfractions in Peaks I and III.

G1- and S-phase synthesis of histone H1 subtypes from mouse NIH fibroblasts and rat C6 glioma cells

Biochemistry ◽  
1993 ◽  
Vol 32 (4) ◽  
pp. 1188-1193 ◽  
Author(s):  
Heribert Talasz ◽  
Wilfried Helliger ◽  
Bernd Puschendorf ◽  
Herbert Lindner
Keyword(s):  
Glioma Cells ◽  
Histone H1 ◽  
C6 Glioma ◽  
S Phase ◽  
C6 Glioma Cells ◽  
Phase Synthesis ◽  
Rat C6 Glioma
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