Evidence map›Paper›PMID 30429328›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Histone tails decrease N7-methyl-2'-deoxyguanosine depurination and yield DNA-protein cross-links in nucleosome core particles and cells.

Kun Yang, Daeyoon Park, Natalia Y Tretyakova, Marc M Greenberg

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.1field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

31 citing papers in PubMed, 52 citations in OpenAlex.

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  18. Targeting DNA-Protein CrosslinksFrontiers in molecular biosciences · 2022
    Review
  19. DNA polymerases η and κ bypass NThe Journal of biological chemistry · 2021
    Article
  20. A chemical field guide to histone nonenzymatic modifications.Current opinion in chemical biology · 2021
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Kun YangDepartment of Chemistry, Johns Hopkins University, Baltimore, MD 21218.
Daeyoon ParkDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Twin Cities, Minneapolis, MN 55417.
Natalia Y TretyakovaDepartment of Medicinal Chemistry, University of Minnesota, Twin Cities, Minneapolis, MN 55417.
Marc M GreenbergDepartment of Chemistry, Johns Hopkins University, Baltimore, MD 21218; mgreenberg@jhu.edu.ORCID 0000-0002-5786-6118
Johns Hopkins University · USUniversity of Minnesota · US

Funding

Repair, Replication, and Detection of Oxidatively Damaged DNAR01GM063028 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREENBERG, MARC M · 2002 to 2018
$5.4M
DNA Protein Cross-Links:Cellular Effects and Repair MechanismsR01ES023350 · NIEHS · UNIVERSITY OF MINNESOTA · PI CAMPBELL, COLIN R, TRETYAKOVA, NATALIA Y · 2014 to 2023
$5.0M
Acquisition of GE Typhoon FLA9500 Variable Mode ImagerS10OD021567 · OD · JOHNS HOPKINS UNIVERSITY · PI MCCAFFERY, J. MICHAEL · 2017 to 2017
$147k
NIEHS NIH HHS R01 ES023350NIGMS NIH HHS R01 GM063028NIH HHS S10 OD021567
6 · The paper itself

Abstract

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,

Indexed as

Amino Acid MotifsAnimalsCell LineCricetinaeDeoxyguanosineDNAHistonesNucleic Acid ConformationNucleosomesProteinsDeoxyguanosineDNAHistonesNucleosomesProteinsDNA alkylationDNA damageDNA–protein cross-linksnucleic acidsnucleosomes

Identifiers

PMID30429328
PMCPMC6275548
OpenAlexW2901218982

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.