scholarly journals Reactivity of the Major Product of C5′-Oxidative DNA Damage in Nucleosome Core Particles

ChemBioChem ◽  
2019 ◽  
Vol 20 (5) ◽  
pp. 672-676
Author(s):  
Anup Rana ◽  
Kun Yang ◽  
Marc M. Greenberg
Keyword(s):  
Dna Damage ◽  
Oxidative Dna Damage ◽  
Major Product ◽  
Nucleosome Core ◽  
Nucleosome Core Particles ◽  
Core Particles

scholarly journals DNA Damage by Histone Radicals in Nucleosome Core Particles

2014 ◽  
Vol 136 (18) ◽  
pp. 6562-6565 ◽  
Author(s):  
Chuanzheng Zhou ◽  
Marc M. Greenberg
Keyword(s):  
Dna Damage ◽  
Nucleosome Core ◽  
Nucleosome Core Particles ◽  
Core Particles

scholarly journals Histones participate in base excision repair of 8-oxodGuo by transiently cross-linking with active repair intermediates in nucleosome core particles

2020 ◽  
Author(s):  
Mengtian Ren ◽  
Mengdi Shang ◽  
Huawei Wang ◽  
Zhen Xi ◽  
Chuanzheng Zhou
Keyword(s):  
Base Excision Repair ◽  
Oxidative Dna Damage ◽  
Excision Repair ◽  
Cross Linking ◽  
Nucleosome Core ◽  
Nucleosome Core Particles ◽  
Lyase Activity ◽  
Base Excision ◽  
Ap Lyase ◽  
Core Particles

Abstract 8-Oxo-7,8-dihydro-2′-deoxyguanosine (8-oxodGuo) is a biomarker of oxidative DNA damage and can be repaired by hOGG1 and APE1 via the base excision repair (BER) pathway. In this work, we studied coordinated BER of 8-oxodGuo by hOGG1 and APE1 in nucleosome core particles and found that histones transiently formed DNA-protein cross-links (DPCs) with active repair intermediates such as 3′-phospho-α,β-unsaturated aldehyde (PUA) and 5′-deoxyribosephosphate (dRP). The effects of histone participation could be beneficial or deleterious to the BER process, depending on the circumstances. In the absence of APE1, histones enhanced the AP lyase activity of hOGG1 by cross-linking with 3′-PUA. However, the formed histone-PUA DPCs hampered the subsequent repair process. In the presence of APE1, both the AP lyase activity of hOGG1 and the formation of histone-PUA DPCs were suppressed. In this case, histones could catalyse removal of the 5′-dRP by transiently cross-linking with the active intermediate. That is, histones promoted the repair by acting as 5′-dRP lyases. Our findings demonstrate that histones participate in multiple steps of 8-oxodGuo repair in nucleosome core particles, highlighting the diverse roles that histones may play during DNA repair in eukaryotic cells.

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

scholarly journals Repackaging DNA: From Nucleosome Core Particles to Protamine Loops

2020 ◽  
Vol 118 (3) ◽  
pp. 226a
Author(s):  
Yuxing Ma ◽  
Obinna Ukogu ◽  
Ashley Carter
Keyword(s):  
Nucleosome Core ◽  
Nucleosome Core Particles ◽  
Core Particles

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
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