The assembly of an H2A2,H2B2,H3,H4 hexamer onto DNA under conditions of physiological ionic strength.

Ellison, M.; Pulleyblank, David E.

doi:10.1016/s0021-9258(17)44117-2

Cited by 11 publications

(5 citation statements)

References 49 publications

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“…Despite the internal differences between P3a and P3b particles, they cannot readily be distinguished by their physical properties. P3b particles are compact since their sedimentation properties are identical with those of P3a particles (Ellison & Pulleyblank, 1983a). The DNA folding around P3a and P3b nucleosome cores also appears to be similar as indicated by their indistinguishable CD spectra and thermal denaturation profiles (Ellison & Pulleyblank, 1983b).…”

Section: Discussionmentioning

confidence: 92%

“…hexamer particle which contains 92-102 bp of DNA (Ellison & Pulleyblank, 1983a). The yield of the hexameric P2 particle decreased when H3 was modified with either APAB or APTP…”

Section: Resultsmentioning

confidence: 99%

“…The four core histones are present in P3b samples in equimolar ratios (Ellison & Pulleyblank, 1983a). If the P3b population includes particles with the composition (H3-H4)3/H2A/H2B, a compensating octameric H2A-H2B rich particle would also have to be present.…”

Section: Discussionmentioning

confidence: 99%

“…The complex was annealed for 2 h at 23 °C, centrifuged to remove insoluble material, and then diluted to a final NaCl concentration of 0.15 M with 3 volumes of 20 mM Tris-HCl, (pH 8.0)/1 mM PMSF before digestion with micrococcal nuclease as described for P2 and P3b. Nucleohistone particles were concentrated by ultrafiltration and separated by sedimentation through 5-20% sucrose gradients (Ellison & Pulleyblank, 1983a).…”

Section: Methodsmentioning

confidence: 99%

“…Lanes excised from the first-dimension 15% SDS-polyacrylamide gels were soaked for 30 min in 0.1 M /3-mercaptoethanol in 0.125 M Tris-HCl, pH 6.8 (stacking gel buffer), to reverse the cross-links and then placed across the top of another 15% SDS-polyacrylamide gel for electrophoresis in the second dimension. Histones were visualized by silver staining as described in Ellison and Pulleyblank (1983a).…”

Section: Methodsmentioning

confidence: 99%

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H3 Cys-110 is in close proximity to the C-terminal regions of H2B and H4 in a nucleosome core with an altered internal arrangement of histones

Kahr

Lewis²,

Pulleyblank³

1990

Biochemistry

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A particle obtained by nuclease digestion of nucleohistone complexes prepared by direct mixing of histones with DNA in 0.15 M NaCl was indistinguishable by composition and physical properties from nucleosome cores prepared under the same conditions from nucleohistone preannealed in 0.6 M NaCl. We show here that different photo-cross-links form when these particles are prepared from H3 labeled with photoaffinity reagents on the unique histone H3 cysteine. H3-H3 histone dimers were dominant when the particles were prepared by dilution of the nucleohistone from 0.6 M NaCl while H3-H2B and H3-H4 histone dimers were prominent if the nucleohistone complex was prepared directly in 0.15 M NaCl. Peptide mapping of the novel H3-H4 and H3-H2B dimers showed that Cys-110 of histone H3 is cross-linked to the 18 amino acid C-terminal end of H4 or to the 66 amino acid C-terminal half of H2B.

show abstract

Section: Discussionmentioning

confidence: 92%

“…hexamer particle which contains 92-102 bp of DNA (Ellison & Pulleyblank, 1983a). The yield of the hexameric P2 particle decreased when H3 was modified with either APAB or APTP…”

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 3 more Smart Citations

H3 Cys-110 is in close proximity to the C-terminal regions of H2B and H4 in a nucleosome core with an altered internal arrangement of histones

Kahr

Lewis²,

Pulleyblank³

1990

Biochemistry

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Assembly of nucleosome-like structures mediated by cauliflower DNA topoisomerase

1989

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Nucleosome-like structures have been efficiently assembled in vitro by interaction of cauliflower histones, pBR322 DNA and cauliflower DNA topoisomerase, as assayed by supercoiling of relaxed circular DNA and by digestion with micrococcal nuclease. The optimum ionic strength for supercoiling was 150 mM KCl and the optimum weight ratio of histone to DNA was approximately 1.0. Four histones, H2A, H2B, H3 and H4, were necessary for the optimum assembling conditions, and the nucleosomes assembled protected DNA fragments of approximately 150 bp in length. It was found that cauliflower DNA topoisomerase acts not only as a DNA-relaxing enzyme but also as a chaperon factor for nucleosome assembly.

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Crystal structure of the nucleosome core particle at 16 Å resolution

Bentley

Lewit-Bentley

Finch

et al. 1984

Journal of Molecular Biology

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The assembly of an H2A2,H2B2,H3,H4 hexamer onto DNA under conditions of physiological ionic strength.

Cited by 11 publications

References 49 publications

H3 Cys-110 is in close proximity to the C-terminal regions of H2B and H4 in a nucleosome core with an altered internal arrangement of histones

H3 Cys-110 is in close proximity to the C-terminal regions of H2B and H4 in a nucleosome core with an altered internal arrangement of histones

Assembly of nucleosome-like structures mediated by cauliflower DNA topoisomerase

Crystal structure of the nucleosome core particle at 16 Å resolution

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