scholarly journals A Dynamic View of the Interaction of Histone Tails with Clustered Abasic Sites in a Nucleosome Core Particle

Author(s):  
Emmanuelle Bignon ◽  
Natacha Gillet ◽  
Tao Jiang ◽  
Christophe Morell ◽  
Elise Dumont
Biochemistry ◽  
2013 ◽  
Vol 52 (12) ◽  
pp. 2157-2164 ◽  
Author(s):  
Jonathan T. Sczepanski ◽  
Chuanzheng Zhou ◽  
Marc M. Greenberg

2005 ◽  
Vol 83 (4) ◽  
pp. 468-476 ◽  
Author(s):  
Michael S Cosgrove ◽  
Cynthia Wolberger

Patterns of histone post-translational modifications correlate with distinct chromosomal states that regulate access to DNA, leading to the histone-code hypothesis. However, it is not clear how modification of flexible histone tails leads to changes in nucleosome dynamics and, thus, chromatin structure. The recent discovery that, like the flexible histone tails, the structured globular domain of the nucleosome core particle is also extensively modified adds a new and exciting dimension to the histone-code hypothesis, and calls for the re-examination of current models for the epigenetic regulation of chromatin structure. Here, we review these findings and other recent studies that suggest the structured globular domain of the nucleosome core particle plays a key role regulating chromatin dynamics.Key words: histones, histone code, modifications, epigenetic, chromatin, nucleosome, dynamics, regulated nucleosome mobility, core, archaeal, combinatorial switch, histone octamer.


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

2000 ◽  
Vol 28 (4) ◽  
pp. 373-376 ◽  
Author(s):  
R. Negri ◽  
M. Buttinelli ◽  
G. Panetta ◽  
V. De Arcangelis ◽  
E. Di Mauro ◽  
...  

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.


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

1984 ◽  
pp. 105-117
Author(s):  
Graham A. Bentley ◽  
John T. Finch ◽  
Anita Lewit-Bentley ◽  
Michel Roth

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