Role of Histone Tails in the Conformation and Interactions of Nucleosome Core Particles†

Biochemistry ◽  
2004 ◽  
Vol 43 (16) ◽  
pp. 4773-4780 ◽  
Author(s):  
Aurélie Bertin ◽  
Amélie Leforestier ◽  
Dominique Durand ◽  
Françoise Livolant
Keyword(s):  
Histone Tails ◽  
Nucleosome Core ◽  
Nucleosome Core Particles ◽  
Core Particles

scholarly journals Dynamic networks observed in the nucleosome core particles couple the histone globular domains with DNA

2020 ◽  
Vol 3 (1) ◽  
Author(s):  
Xiangyan Shi ◽  
Chinmayi Prasanna ◽  
Aghil Soman ◽  
Konstantin Pervushin ◽  
Lars Nordenskiöld
Keyword(s):  
Dynamic Networks ◽  
Structural Features ◽  
Epigenetic Changes ◽  
Internal Dynamics ◽  
Histone Tails ◽  
Multiple Timescales ◽  
Nucleosome Core ◽  
The Core ◽  
Nucleosome Core Particles ◽  
Core Particles

Abstract The dynamics of eukaryotic nucleosomes are essential in gene activity and well regulated by various factors. Here, we elucidated the internal dynamics at multiple timescales for the human histones hH3 and hH4 in the Widom 601 nucleosome core particles (NCP), suggesting that four dynamic networks are formed by the residues exhibiting larger-scale μs-ms motions that extend from the NCP core to the histone tails and DNA. Furthermore, despite possessing highly conserved structural features, histones in the telomeric NCP exhibit enhanced μs-ms dynamics in the globular sites residing at the identified dynamic networks and in a neighboring region. In addition, higher mobility was observed for the N-terminal tails of hH3 and hH4 in the telomeric NCP. The results demonstrate the existence of dynamic networks in nucleosomes, through which the center of the core regions could interactively communicate with histone tails and DNA to potentially propagate epigenetic changes.

scholarly journals Histone tails decrease N7-methyl-2′-deoxyguanosine depurination and yield DNA–protein cross-links in nucleosome core particles and cells

2018 ◽  
Vol 115 (48) ◽  
pp. E11212-E11220 ◽  
Author(s):  
Kun Yang ◽  
Daeyoon Park ◽  
Natalia Y. Tretyakova ◽  
Marc M. Greenberg
Keyword(s):  
Alkylating Agents ◽  
Histone Variants ◽  
Site Formation ◽  
Abasic Site ◽  
Histone Tails ◽  
Nucleosome Core ◽  
Nucleosome Core Particles ◽  
Cross Links ◽  
Positively Charged ◽  
Core Particles

Monofunctional alkylating agents preferentially react at the N7 position of 2′-deoxyguanosine in duplex DNA. Methylated DNA, such as that produced by methyl methanesulfonate (MMS) and temozolomide, exists for days in organisms. The predominant consequence of N7-methyl-2′-deoxyguanosine (MdG) is widely believed to be abasic site (AP) formation via hydrolysis, a process that is slow in free DNA. Examination of MdG reactivity within nucleosome core particles (NCPs) provided two general observations. MdG depurination rate constants are reduced in NCPs compared with when the identical DNA sequence is free in solution. The magnitude of the decrease correlates with proximity to the positively charged histone tails, and experiments in NCPs containing histone variants reveal that positively charged amino acids are responsible for the decreased rate of abasic site formation from MdG. In addition, the lysine-rich histone tails form DNA–protein cross-links (DPCs) with MdG. Cross-link formation is reversible and is ascribed to nucleophilic attack at the C8 position of MdG. DPC and retarded abasic site formation are observed in NCPs randomly damaged by MMS, indicating that these are general processes. Histone–MdG cross-links were also detected by mass spectrometry in chromatin isolated from V79 Chinese hamster lung cells treated with MMS. The formation of DPCs following damage by a monofunctional alkylating agent has not been reported previously. These observations reveal the possibility that such DPCs may contribute to the cytotoxicity of monofunctional alkylating agents, such as MMS, N-methyl-N-nitrosourea, and temozolomide.

scholarly journals The Influence of Ionic Environment and Histone Tails on Columnar Order of Nucleosome Core Particles

2016 ◽  
Vol 110 (8) ◽  
pp. 1720-1731 ◽  
Author(s):  
Nikolay V. Berezhnoy ◽  
Ying Liu ◽  
Abdollah Allahverdi ◽  
Renliang Yang ◽  
Chun-Jen Su ◽  
...  
Keyword(s):  
Histone Tails ◽  
Nucleosome Core ◽  
Ionic Environment ◽  
Nucleosome Core Particles ◽  
Core Particles

Polyamines and acetylpolyamines increase the stability and alter the conformation of nucleosome core particles

Biochemistry ◽  
1987 ◽  
Vol 26 (12) ◽  
pp. 3643-3649 ◽  
Author(s):  
James E. Morgan ◽  
James W. Blankenship ◽  
Harry R. Matthews
Keyword(s):  
Nucleosome Core ◽  
Nucleosome Core Particles ◽  
The Stability ◽  
Core Particles
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