Literature DB >> 29631253

Synergistic effects of H3 and H4 nucleosome tails on structure and dynamics of a lesion-containing DNA: Binding of a displaced lesion partner base to the H3 tail for GG-NER recognition.

Yuqin Cai1, Iwen Fu1, Nicholas E Geacintov2, Yingkai Zhang3, Suse Broyde4.   

Abstract

How DNA lesions in nucleosomes are recognized for global genome nucleotide excision repair (GG-NER) remains poorly understood, and the roles that histone tails may play remains to be established. Histone H3 and H4 N-terminal tails are of particular interest as their acetylation states are important in regulating nucleosomal functions in transcription, replication and repair. In particular the H3 tail has been the focus of recent attention as a site for the interaction with XPC, the GG-NER lesion recognition factor. Here we have investigated how the structure and dynamics of the DNA lesion cis-B[a]P-dG, derived from the environmental carcinogen benzo[a]pyrene (B[a]P), is impacted by the presence of flanking H3 and H4 tails. This lesion is well-repaired by GG-NER, and adopts a base-displaced/intercalated conformation in which the lesion partner C is displaced into the major groove. We used molecular dynamics simulations to obtain structural and dynamic characterizations for this lesion positioned in nucleosomal DNA so that it is bracketed by the H3 and H4 tails. The H4 tail was studied in unacetylated and acetylated states, while the H3 tail was unacetylated, its state when it binds XPC (Kakumu, Nakanishi et al., 2017). Our results reveal that upon acetylation, the H4 tail is released from the DNA surface; the H3 tail then forms a pocket that induces flipping and capture of the displaced lesion partner base C. This reveals synergistic effects of the behavior of the two tails. We hypothesize that the dual capability of the H3 tail to sense the displaced lesion partner base and to bind XPC could foster recognition of this lesion by XPC for initiation of GG-NER in nucleosomes.
Copyright © 2018 Elsevier B.V. All rights reserved.

Entities:  

Keywords:  DNA adduct; Histone tails; Lysine acetylation; MD simulations; Nucleosome core particle; Nucleotide excision repair

Mesh:

Substances:

Year:  2018        PMID: 29631253      PMCID: PMC5911426          DOI: 10.1016/j.dnarep.2018.02.009

Source DB:  PubMed          Journal:  DNA Repair (Amst)        ISSN: 1568-7856


  65 in total

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Journal:  J Mol Biol       Date:  2008-04-29       Impact factor: 5.469

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Authors:  Orlando D Schärer
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7.  Xeroderma pigmentosum group C protein interacts with histones: regulation by acetylated states of histone H3.

Authors:  Erina Kakumu; Seiya Nakanishi; Hiromi M Shiratori; Akari Kato; Wataru Kobayashi; Shinichi Machida; Takeshi Yasuda; Naoko Adachi; Naoaki Saito; Tsuyoshi Ikura; Hitoshi Kurumizaka; Hiroshi Kimura; Masayuki Yokoi; Wataru Sakai; Kaoru Sugasawa
Journal:  Genes Cells       Date:  2017-02-24       Impact factor: 1.891

8.  Aromatic-proline interactions: electronically tunable CH/π interactions.

Authors:  Neal J Zondlo
Journal:  Acc Chem Res       Date:  2012-11-13       Impact factor: 22.384

9.  Nucleosome Histone Tail Conformation and Dynamics: Impacts of Lysine Acetylation and a Nearby Minor Groove Benzo[a]pyrene-Derived Lesion.

Authors:  Iwen Fu; Yuqin Cai; Nicholas E Geacintov; Yingkai Zhang; Suse Broyde
Journal:  Biochemistry       Date:  2017-03-22       Impact factor: 3.162

10.  Histones H3 and H4 require their relevant amino-tails for efficient nuclear import and replication-coupled chromatin assembly in vivo.

Authors:  Aïda Ejlassi; Vanessa Menil-Philippot; Angélique Galvani; Christophe Thiriet
Journal:  Sci Rep       Date:  2017-06-08       Impact factor: 4.379

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  4 in total

1.  Variable impact of conformationally distinct DNA lesions on nucleosome structure and dynamics: Implications for nucleotide excision repair.

Authors:  Yuqin Cai; Nicholas E Geacintov; Suse Broyde
Journal:  DNA Repair (Amst)       Date:  2019-12-28

2.  Molecular dynamics simulations reveal how H3K56 acetylation impacts nucleosome structure to promote DNA exposure for lesion sensing.

Authors:  Iwen Fu; Nicholas E Geacintov; Suse Broyde
Journal:  DNA Repair (Amst)       Date:  2021-08-08

3.  A chromatin scaffold for DNA damage recognition: how histone methyltransferases prime nucleosomes for repair of ultraviolet light-induced lesions.

Authors:  Corina Gsell; Holger Richly; Frédéric Coin; Hanspeter Naegeli
Journal:  Nucleic Acids Res       Date:  2020-02-28       Impact factor: 16.971

4.  Comparison of the Base Excision and Direct Reversal Repair Pathways for Correcting 1,N6-Ethenoadenine in Strongly Positioned Nucleosome Core Particles.

Authors:  Paul J Caffrey; Raadhika Kher; Ke Bian; Deyu Li; Sarah Delaney
Journal:  Chem Res Toxicol       Date:  2020-05-01       Impact factor: 3.739

  4 in total

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