Similarity of chromatin from different tissues

Itzhaki, Ruth F.; Cooper, Helen K.

doi:10.1016/0022-2836(73)90533-0

Cited by 32 publications

(8 citation statements)

References 15 publications

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“…It has been reported by Itzhaki & Cooper (1973) that in chromatin from different sources 42 to 47 ~ of the DNA-phosphate groups are available for binding poly-lysine, which means that only about 5o to 6o ~ of the DNA-phosphate groups bind to the histones. As the adenovirus nucleoprotein is very basic it may bind to DNA-phosphates in a similar way as the histones.…”

Section: Discussionmentioning

confidence: 99%

Electron Microscopy of Adenovirus Cores

Nermut¹,

Harpst²,

Russell³

1975

Journal of General Virology

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SUMMARYAdenovirus type 5 'cores' prepared by heating in the presence of deoxycholate and partially purified on a glycerol density gradient could be visualized as roughly isometrical particles with a condensed centre from which twisted filaments or loops of DNA emanated. This compact structure was readily dispersed by spreading on distilled water or by treatment with EDTA, Nonidet, DNase or trypsin. Spreading with Nonidet was particularly effective in unfolding the cores and revealing long filaments about IOO A thick presumably of the virus nucleoprotein. Subunits (about 30 to 60 A in diam.) could be seen free in the DNase-treated cores, suggesting a particulate nature of one or both of the core proteins.

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Section: Discussionmentioning

confidence: 99%

Electron Microscopy of Adenovirus Cores

Nermut¹,

Harpst²,

Russell³

1975

Journal of General Virology

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“…The second assumption (that polylysine does not displace chromosomal protein) is supported by evidence that soluble protein does not appear when chromatin is titrated with polylysine (1,3,19,20). (This fact only holds true so long as the neutralization point is not exceeded.)…”

Section: Discussionmentioning

confidence: 99%

Isolation and characterization of the DNA fraction of rat liver chromatin which binds polylysine

1975

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The structure of eukaryotic chromatin has been investigated by isolating and analyzing the "accessible" DNA fraction of rat liver chromatin. This DNA fraction has been isolated by titrating the chromatin with the protese-resistant D isomer of polylysine to bind the "accessible" DNA sites. After removal of chromosomal proteins by digestion with pronase, all DNA not protected from attack by bound polylysine was removed by digestion with DNase. Even after exhaustive treatment with pronase and DNase approximately 30% of the chromatin DNA remains resistant to nuclease attack. Analysis of the isolated DNA shows it to be mainly double-stranded with an average size of 200-250 base pairs. The DNA is slightly A-T rich and contains both repetitive and "single-copy" nuleotide sequences. The results suggest that there are extensive regions in chromatin where the DNA is not tightly complexed with protein. Furthermore, the DNA of these regions is similar in gross properties to the DNA of the total genome.

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“…NaCl was added to a final 1.0 M concentration and DNA was extracted and purified by the phenol method of Marmur [25]. Liver chromatin was prepared from isolated liver nuclei [27] by the method of Itzhaki and Cooper [16] but repeated 3 times the final washing procedure. Sperm DNA was obtained and purified by the method of Marmur [25] as modified by Hernández-Pérez et al [14].…”

Section: Methodsmentioning

confidence: 99%

Participation of Dna Structure on Sperm Chromatin Organization

Fuentes-Mascorro

Vergara‐Onofre

Mercado³

et al. 2000

Archives of Andrology

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The in vitro interaction between purified bovine liver and sperm DNA with somatic histones, to form nucleosomes, and with bovine and salmon protamines were studied. DNAse or microccocal nuclease digestion of liver DNA-histone reassociated chromatin produced the expected polynucleosome type of fragments. Electrophoretic patterns of digested sperm-DNA nucleosomes were different. Micrococcal nuclease digestion produced mainly fragments smaller than 100 bp and some nucleosome-type particles. Under DNAse activity most of the products were smaller than 100 bp, indicating an increased susceptibility of the sperm DNA-histone complexes to the hydrolytic activity of both nucleases, particularly toward DNAse I. This differential susceptibility was confirmed by sucrose gradient spectrophotometric analysis. Acridine orange (AO) staining of histone-DNA reassociated nucleosomes showed significant differences in fluorescence intensity, sperm DNA-histone complexes being almost twice as fluorescent as liver DNA-histone complexes. On the contrary, liver DNA/protamine complexes stained with AO were consistently more fluorescent than sperm DNA-protamine complexes. Finally, no differences in either fluorescence intensity or spectra were observed when liver and sperm DNA were stained with AO after interaction with salmon protamines. The data suggest that sperm DNA has important structural characteristics that differentiates it from somatic DNA. These differences seem to be species specific and must surely play an important role on the determination of the dramatic sequence of that participates sperm chromatin organization.

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Similarity of chromatin from different tissues

Cited by 32 publications

References 15 publications

Electron Microscopy of Adenovirus Cores

Electron Microscopy of Adenovirus Cores

Isolation and characterization of the DNA fraction of rat liver chromatin which binds polylysine

Participation of Dna Structure on Sperm Chromatin Organization

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