Stable DNA−Protein Cross-Links Are Products of DNA Charge Transport in a Nucleosome Core Particle†

Biochemistry ◽  
2007 ◽  
Vol 46 (38) ◽  
pp. 10745-10755 ◽  
Author(s):  
Chad C. Bjorklund ◽  
William B. Davis
Keyword(s):  
Charge Transport ◽  
Core Particle ◽  
Nucleosome Core Particle ◽  
Nucleosome Core ◽  
Dna Charge Transport ◽  
Cross Links

scholarly journals Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions

2001 ◽  
Vol 20 (18) ◽  
pp. 5207-5218 ◽  
Author(s):  
Cindy L. White ◽  
Robert K. Suto ◽  
Karolin Luger
Keyword(s):  
Core Particle ◽  
Nucleosome Core Particle ◽  
Nucleosome Core

Helical repeat of DNA in the nucleosome core particle

2000 ◽  
Vol 28 (4) ◽  
pp. 373-376 ◽  
Author(s):  
R. Negri ◽  
M. Buttinelli ◽  
G. Panetta ◽  
V. De Arcangelis ◽  
E. Di Mauro ◽  
...  
Keyword(s):  
Dna Sequences ◽  
Linker Histone ◽  
Core Particle ◽  
Nucleosome Core Particle ◽  
Apparent Paradox ◽  
Nucleosome Core ◽  
Nucleosome Core Particles ◽  
High Affinity Site ◽  
Hydroxyl Radical Cleavage ◽  
Radical Cleavage

Although the crystal structure of nucleosome core particle is essentially symmetrical in the vicinity of the dyad, the linker histone binds asymmetrically in this region to select a single high-affinity site from potentially two equivalent sites. To try to resolve this apparent paradox we mapped to base-pair resolution the dyads and rotational settings of nucleosome core particles reassembled on synthetic tandemly repeating 20 bp DNA sequences. In agreement with previous observations, we observed (1) that the helical repeat on each side of the dyad cluster is 10 bp maintaining register with the sequence repeat and (2) that this register changes by 2 bp in the vicinity of the dyad. The additional 2 bp required to effect the change in the rotational settings is accommodated by an adjustment immediately adjacent to the dyad. At the dyad the hydroxyl radical cleavage is asymmetric and we suggest that the inferred structural asymmetry could direct the binding of the linker histone to a single preferred site.

scholarly journals 3.9 Å structure of the nucleosome core particle determined by phase-plate cryo-EM

2016 ◽  
Vol 44 (17) ◽  
pp. 8013-8019 ◽  
Author(s):  
Eugene Y.D. Chua ◽  
Vinod K. Vogirala ◽  
Oviya Inian ◽  
Andrew S.W. Wong ◽  
Lars Nordenskiöld ◽  
...  
Keyword(s):  
Phase Plate ◽  
Core Particle ◽  
Nucleosome Core Particle ◽  
Nucleosome Core

The Crystal Structure of the Nucleosome Core Particle by Contrast Variation

1984 ◽  
pp. 105-117
Author(s):  
Graham A. Bentley ◽  
John T. Finch ◽  
Anita Lewit-Bentley ◽  
Michel Roth
Keyword(s):  
Crystal Structure ◽  
Core Particle ◽  
Nucleosome Core Particle ◽  
Contrast Variation ◽  
Nucleosome Core
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