Aberrant RNA methylation triggers recruitment of an alkylation repair complex
Open accessAbstract
Central to genotoxic responses is their ability to sense highly specific signals to activate the appropriate repair response. We previously reported that the activation of the ASCC-ALKBH3 repair pathway is exquisitely specific to alkylation damage in human cells. Yet the mechanistic basis for the selectivity of this pathway was not immediately obvious. Here, we demonstrate that RNA but not DNA alkylation is the initiating signal for this process. Aberrantly methylated RNA is sufficient to recruit ASCC, while an RNA dealkylase suppresses ASCC recruitment during chemical alkylation. In turn, recruitment of ASCC during alkylation damage, which is mediated by the E3 ubiquitin ligase RNF113A, suppresses transcription and R-loop formation. We further show that alkylated pre-mRNA is sufficient to activate RNF113A E3 ligase in vitro in a manner dependent on its RNA binding Zn-finger domain. Together, our work identifies an unexpected role for RNA damage in eliciting a specific response to genotoxins.
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Claims the paper makes
5 of 10 cited sources checked · 1 supported · 0 flagged · accuracy not yet measured
- Background
Earlier work from the authors established that human ALKBH3 is coupled to the ASCC helicase and is recruited during alkylation damage.
“We previously showed that human ALKBH3 is coupled to the ASCC helicase, which is specifically recruited during alkylation damage to nuclear speckle bodies, corresponding to regions of RNA polymerase II transcript processing (Brickner et al., 2017).”
Quote in the paperNot yet classified1 of 1 sources checked- cites Brickner et al., 2017 source
The paper reports that ALKBH3 functions with the ASCC helicase complex and co-localizes with ASCC3 in foci after alkylation damage (Abstract; page unavailable). It also reports that ASCC foci co-localize with splicing factors and elongating RNA polymerase II, but does not identify those foci as nuclear speckle bodies or establish them as regions of RNA polymerase II transcript processing. (LLM, conf=0.83)
Experimental — accuracy not yet measured
- Method
An RNA-specific AlkB enzyme from blueberry scorch disease virus was cloned and used as a nuclear tool to test whether RNA damage is required for ASCC recruitment.
“We cloned and characterized an AlkB demethylase from blueberry scorch disease virus (BsV), an RNA virus (van den Born et al., 2008).”
Quote in the paperNot yet classified1 of 1 sources checked- cites van den Born et al., 2008 source
- Finding
The catalytic mutants of METTL8 failed to recruit ASCC3 to nucleoli.
“Conversely, two catalytic mutations targeting the putative SAM-binding domain of METTL8 (D’Silva et al., 2011; Noma et al., 2011) (G204A/G206A and D230A; Supplemental Figure S2a–S2c) failed to recruit ASCC3 to nucleoli”
Quote in the paperNot yet classified2 of 2 sources checked- cites D’Silva et al., 2011 source
The citation is attached to the description of a putative SAM-binding domain, not directly to the recruitment result. The Discussion describes a conserved SAM-methyltransferase domain in yeast Trm140p, but our copy does not address METTL8 catalytic mutants, ASCC3, or nucleolar recruitment (searched those terms and the specified mutations). (LLM, conf=0.78)
Experimental — accuracy not yet measured - cites Noma et al., 2011 source
The Discussion describes a conserved Ado-Met (SAM)-binding motif in ABP140/TRM140, and the section on METTL2B identifies the motif in a human ortholog. The paper does not identify a SAM-binding domain in METTL8 or examine the specified METTL8 mutations. It also does not address ASCC3 recruitment to nucleoli; the citation is attached to the domain description, not that reported outcome. (LLM, conf=0.83)
Experimental — accuracy not yet measured
- Finding
A substantial fraction of RNF113A-associated ubiquitin linkages after MMS were K63-linked.
“This showed that a significant portion of the ubiquitin linkage associated with RNF113A activation was K63-linked”
Quote in the paperNot yet classified1 of 1 sources checked- cites Brickner et al., 2017 source
The main-text passage indexed under Abstract (page unavailable) reports that K63R ubiquitin abrogated RNF113A-dependent chain elongation in vitro, supporting a role for K63 linkages. Extended Data Figure 10 (page unavailable) describes ubiquitination assays after MMS treatment, but neither passage establishes what fraction of RNF113A-associated linkages after MMS were K63-linked. (LLM, conf=0.85)
Experimental — accuracy not yet measured
- Finding
It reports that damaged RNA is sufficient to bring in ASCC, and that an RNA dealkylase can block that recruitment during chemical alkylation.
“Aberrantly methylated RNA is sufficient to recruit ASCC, while an RNA dealkylase suppresses ASCC recruitment during chemical alkylation.”
Quote in the paperNot yet classified
- Finding
The paper concludes that aberrant RNA methylation, not DNA alkylation, initiates recruitment of the ASCC-ALKBH3 pathway.
“Here, we demonstrate that RNA but not DNA alkylation is the initiating signal for this process.”
Quote in the paperNot yet classified - Finding
The study finds that ASCC recruitment during alkylation, through RNF113A, reduces transcription and R-loop formation.
“recruitment of ASCC during alkylation damage, which is mediated by the E3 ubiquitin ligase RNF113A, suppresses transcription and R-loop formation.”
Quote in the paperNot yet classified - Finding
The authors show that alkylated pre-mRNA can activate RNF113A E3 ligase in vitro through its RNA-binding zinc-finger domain.
“alkylated pre-mRNA is sufficient to activate RNF113A E3 ligase in vitro in a manner dependent on its RNA binding Zn-finger domain.”
Quote in the paperNot yet classified - Finding
TRMT61A, another RNA methyltransferase, also recruited ASCC3 and ALKBH3, but not ALKBH2, supporting specificity for the ASCC-ALKBH3 pathway.
“TRMT61A also resulted in recruitment of ASCC3 to these same regions in a manner that depended on the TRMT61A catalytic domain”
Quote in the paperNot yet classified0 of 2 sources checked - Finding
Targeting wild-type METTL8 to the nucleus recruited ASCC3 to nucleolar regions, whereas catalytic mutants did not.
“Ectopic expression of wildtype METTL8-NLS induced recruitment of the ASCC3 helicase to nucleolar regions”
Quote in the paperNot yet classified - Finding
BsV-AlkB demethylated an m1A RNA oligonucleotide but not an identically sequenced DNA substrate.
“we confirmed that BsV-AlkB can demethylate a m1A-modified RNA olignonucleotide but not a DNA substrate with the identical sequence”
Quote in the paperNot yet classified - Finding
METTL8 was active on an RNA substrate in vitro, but not on the matching DNA substrate.
“Using LC-MS/MS METTL8 was found to be active only on a ssRNA substrate in vitro; no activity was found on the same ssDNA substrate”
Quote in the paperNot yet classified0 of 2 sources checked- cites Xu et al., 2017
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
- cites Aas et al., 2003 source
- Finding
Expressing nuclear BsV-AlkB reduced MMS-induced ASCC2 foci to baseline, indicating that RNA alkylation is needed for ASCC2 foci formation.
“BsV-AlkB-NLS expression significantly reduced HA-ASCC2 foci formation to background levels following MMS-induced alkylation damage”
Quote in the paperNot yet classified - Finding
The authors conclude that RNA alkylation is necessary for MMS-induced ASCC2 foci formation.
“indicating that RNA alkylation is necessary for MMS-induced ASCC2 foci formation.”
Quote in the paperNot yet classified - Finding
The authors infer that ASCC3 may repress or degrade certain transcripts during alkylation stress.
“Thus ASCC3 potentially represses or degrades certain transcripts.”
Quote in the paperNot yet classified - Finding
Mutation or deletion of the RNF113A RING domain reduced its MMS-induced ubiquitination, supporting autoubiquitination.
“Deletion or mutation of the RING domain significantly reduced RNF113A ubiquitination upon MMS treatment, indicating that this represents bona fide autoubiquitination”
Quote in the paperNot yet classified - Finding
RNA-Seq showed that MMS altered many mRNAs rather than causing a global transcriptional shutdown.
“RNA-Seq analysis revealed that while a global transcript downregulation did not occur in response to MMS, many mRNAs were altered under these conditions”
Quote in the paperNot yet classified - Finding
The study finds that ASCC complex recruitment to aberrantly methylated RNA helps limit expression and R-loop formation.
“Our data indicates that the ASCC complex is recruited to sites harboring aberrant RNA methylation to mitigate their expression or induce their turnover, in turn limiting R-loop formation.”
Quote in the paperNot yet classified - Finding
Loss of ASCC3 increased R-loop accumulation after MMS treatment.
“ASCC3 KO cells exhibited greater R-loops compared with controls upon MMS damage”
Quote in the paperNot yet classified - Finding
RNF113A was ubiquitinated in response to MMS but not other tested damaging agents.
“we found that RNF113A was ubiquitinated in response to MMS, but not by other types of damaging agents”
Quote in the paperNot yet classified - Finding
Targeting METTL8 to a reporter locus reduced reporter transcript levels, and this effect required METTL8 catalytic activity.
“targeting METTL8 to this locus significantly reduced transcript levels from this reporter”
Quote in the paperNot yet classified - Background
The molecular basis for why the RNF113A-ASCC-ALKBH3 pathway is selective for alkylation damage was unclear before this study.
“However, the molecular basis for the alkylation damage specificity in the RNF113A-ASCC-ALKBH3 pathway remains unclear.”
Quote in the paperNot yet classified - Method
The authors used quantitative LC-MS/MS to verify that BsV-AlkB is selective for RNA over DNA in the assay conditions used.
“By using quantitative LC-MS/MS, we confirmed that BsV-AlkB can demethylate a m1A-modified RNA olignonucleotide but not a DNA substrate with the identical sequence”
Quote in the paperNot yet classified - Method
Using a locus-targeting reporter system, the authors found that METTL8-induced ASCC3 recruitment depended on METTL8 catalytic activity.
“Here, fusing a degron-tagged METTL8-NLS to mCherry-LacI allowed for targeted recruitment of the methyltransferase to the locus upon induction with the Shield1 ligand”
Quote in the paperNot yet classified0 of 1 sources checked- cites Janicki et al., 2004; Shanbhag et al., 2010
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
- Background
The recruitment of ASCC depends on K63-linked ubiquitination by RNF113A and recognition of that ubiquitin chain by ASCC2.
“The recruitment of this complex requires K63-linked ubiquitination by the RNF113A E3 ubiquitin ligase and recognition of the ubiquitin chain by ASCC2.”
Quote in the paperNot yet classified
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Self-citationThe Molecular Basis of Human ALKBH3 Mediated RNA N 1 ‐methyladenosine (m 1 A) Demethylation
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Self-citationSmall Cell Lung Cancer—An Update on Chemotherapy Resistance
Ying, Q., Fan, R., Shen, Y., Chen, B., Zhang, J., Li, Q., & Shi, X. (2024) · Current Treatment Options in Oncology · doi:10.1007/s11864-024-01245-w · Cited by 24 · see citing works
“Emerging research has indicated that RNF113A can be specifically activated to exert its influence on repairing damages caused by alkylation [86, 87].”
The Emerging Role of RNA Modifications in DNA Double-Strand Break Repair
Jimeno, S., Balestra, F. R., & Huertas, P. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.664872 · Cited by 19 · see citing works
YTHDC1 cooperates with the THO complex to prevent RNA damage-induced DNA breaks
Tsao, N., Lombardi, P. M., Park, A., Olabode, J., Rodell, R., Sun, H., Padmanaban, S., Brickner, J. R., Tsai, M.-S., Pollina, E. A., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2025.02.003 · Cited by 18 · see citing works
Self-citationTownley, B. A., Buerer, L., Tsao, N., Bacolla, A., Mansoori, F., Rusanov, T., Clark, N. E., Goodarzi, N., Schmidt, N., Srivatsan, S. N., et al. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.06.011 · Cited by 15 · see citing works
Self-citationJia, J., Hilal, T., Bohnsack, K. E., Chernev, A., Tsao, N., Bethmann, J., Arumugam, A., Parmely, L., Holton, N., Loll, B., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-37528-3 · Cited by 12 · see citing works
Self-citationSchmidl, D., Jonasson, N. S. W., Menke, A., Schneider, S., & Daumann, L. J. (2022) · ChemBioChem · doi:10.1002/cbic.202100605 · Cited by 14 · see citing works
Tsampoula, M., Tarampoulous, I., Manolakou, T., Ninou, E., & Politis, P. K. (2022) · Stem Cells · doi:10.1093/stmcls/sxac030 · Cited by 11 · see citing works
Chen, H., Ferguson, C., Mitchell, D. C., Risch, I., Titus, A., Paulo, J. A., Hwang, A., Beck, L. P., Lin, T., Gu, W. J., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115231 · Cited by 11 · see citing works
Effect of RNF113A deficiency on oxidative stress-induced NRF2 pathway
Cho, N., Kim, Y., Lee, Y., Choi, D. W., Park, C., Kim, J. H., Kim, K. I., & Kim, K. K. (2024) · Animal Cells and Systems · doi:10.1080/19768354.2024.2349758 · Cited by 10 · see citing works
“Other studies have focused on the function of RNF113A in the repair of DNA alkylation damage (Brickner et al. 2017; Tsao et al. 2021; Lukinovic et al. 2022).”
BackgroundRNA damage and its implications in genome stability
Olatunji, M., & Liu, Y. (2025) · DNA repair · doi:10.1016/j.dnarep.2025.103821 · Cited by 9 · see citing works
Tsao, N., Ashour, M. E., & Mosammaparast, N. (2023) · DNA repair · doi:10.1016/j.dnarep.2023.103564 · Cited by 7 · see citing works
Self-citationThe PARP1–EXD2 axis orchestrates R-loop resolution to safeguard genome stability
Li, Z., Liu, Y., Liu, Y., Zhang, Y., Huen, M. S. Y., Lu, H., Zhang, Z., Zhou, J., Dong, F., Liu, T., et al. (2025) · Nature Chemical Biology · doi:10.1038/s41589-025-01952-x · Cited by 8 · see citing works
“Upon treatment with the alkylating agent MMS (methyl methanesulfonate) to induce R-loop accumulation 41 , there was a noticeable increase in the number of EXD2–S9.”
The epitranscriptome: reshaping the DNA damage response
Kalamara, V., & Garinis, G. A. (2024) · Trends in Cell Biology · doi:10.1016/j.tcb.2024.06.008 · Cited by 7 · see citing works
RNA Damage Responses in Cellular Homeostasis, Genome Stability, and Disease
Zaher, H. S., & Mosammaparast, N. (2024) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-111523-023516 · Cited by 8 · see citing works
Self-citationRapid profiling of DNA replication dynamics using mass spectrometry–based analysis of nascent DNA
Ashour, M. E., Byrum, A. K., Meroni, A., Xia, J., Singh, S. S., Galletto, R., Rosenberg, S. M., Vindigni, A., & Mosammaparast, N. (2023) · The Journal of Cell Biology · doi:10.1083/jcb.202207121 · Cited by 6 · see citing works
“Indeed, we have shown this type of MS can be used to demonstrate association of an RNA-binding protein with alkylated ribo-nucleosides upon methyl methanesulfonate – mediated damage (Tsao et al., 2021; Tsao et al., 2022).”
Self-citationEmerging role of mRNA methylation in regulating the hallmarks of cancer
Sarraf, G., & Chhabra, R. (2022) · Biochimie · doi:10.1016/j.biochi.2022.10.005 · Cited by 6 · see citing works
Trichothiodystrophy: Molecular insights and mechanisms of pathogenicity
Lanzafame, M., Brevi, F., Veniali, G., & Botta, E. (2025) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2025.108555 · Cited by 7 · see citing works
The Secret Life of N1-methyladenosine: A Review on its Regulatory Functions
Nguyen, N. Y. T., Liu, X., Dutta, A., & Su, Z. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169099 · Cited by 5 · see citing works
Tsao, N., Soll, J. M., & Mosammaparast, N. (2022) · STAR Protocols · doi:10.1016/j.xpro.2022.101268 · Cited by 4 · see citing works
Self-citationChiu, C., Hsu, S., Liu, W., Lin, I., Qiu, W., Hsieh, C., & Chou, C. (2025) · Cancer Medicine · doi:10.1002/cam4.71055 · Cited by 4 · see citing works
Tainer, J. A., & Tsutakawa, S. E. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108474 · Cited by 3 · see citing works
“These complexes can furthermore act more like multifunctional molecular machines than linear pathways, as seen for alkylation damage responses, nucleotide excision repair, DNA break repair, and replication fork restart (80, 95, 105, 109, 111 – 118).”
Self-citationYTHDC1 cooperates with the THO complex to prevent RNA damage-induced DNA breaksPreprint
Tsao, N., Olabode, J., Rodell, R., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.14.585107 · Cited by 3 · see citing works
Self-citationZhang, Z., Kotopanova, Z. V., Dang, K., et al. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag080 · Cited by 2 · see citing works
A stress-dependent TRIM28–ALKBH2 feedback loop modulates chemoresistance in NSCLCPreprint
Sun, Z., Deng, Y., Liu, Y., Liu, Z., Li, J., Wu, L., Zeng, L., Feng, X., Miao, L., Sheng, Y., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.21.689678 · Cited by 2 · see citing works
Zhang, Z., Kotopanova, Z. V., Dang, K., Kong, X., Simms, N., Yuen, T. W., Soenmez, A., Beadle, L. F., Hilton, E. N., Qureshi, T., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.01.646554 · Cited by 2 · see citing works
Chen, H., Ferguson, C., Mitchell, D. C., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.10.24.563880 · Cited by 2 · see citing works
Zhang, X., Wang, X., Wang, Q., et al. (2026) · Biomarker Research · doi:10.1186/s40364-025-00867-y · Cited by 1 · see citing works
“ASCC2 is a ubiquitin-binding protein involved in DNA repair [24, 25] and ribosome quality control [26, 27].”
Self-citationRNase H-sensitive accumulation of APOBEC3B in a nucleolus after DNA damage
Saito, Y., Yamamoto, Y., & Yamamoto, F. (2025) · Bioscience Reports · doi:10.1042/bsr20253880 · Cited by 1 · see citing works
When RNA damage induces DNA breaks
Mikičić, I., & Beli, P. (2025) · Trends in Cell Biology · doi:10.1016/j.tcb.2025.03.004 · Cited by 1 · see citing works
Townley, B. A., Buerer, L., Bacolla, A., Rusanov, T., Schmidt, N., Srivatsan, S. N., Clark, N. E., Mansoori, F., Sample, R. A., Brickner, J. R., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.03.515106 · Cited by 1 · see citing works
Self-citation(2022) · doi:10.21203/rs.3.rs-2007381/v1 · Cited by 12 · see citing works
Self-citationSoto-Hidalgo, E., Espejo-Serrano, C., de Arellano, R., González-Vinceiro, L., Marugán-Cardiel, M., Domínguez-García, I., Hortal, A. R., Mateos‐Martín, M. L., García‐Rodríguez, N., Freire, R., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.21.753208
Shi, L., Weng, Y., Ye, L., et al. (2026) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.70970
“Owing to the presence of its RING domain, RNF113A has been identified as functioning as an E3 ubiquitin ligase [8].”
Wang, T., Li, W., Yu, A., et al. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.116840
Ahmad, T., Yang, X., Foucher, A., Ren, L., Tsao, N., Flores, N. M., Wan, J., Belmudes, L., Dubiez, E., Bhowmik, M. C., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.03.697470
Self-citationHuman MutLα activates methylpurine DNA glycosylase to induce alkylation damage cytotoxicityPreprint
Ashour, M. E., Krekeler, E., Bhowmik, M. C., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.15.694403
Self-citationSepich‐Poore, C., Pajdzik, K., Dou, X., et al. (2024) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2024.117905
Self-citationRetractedThe Molecular Basis of Human ALKBH3 Mediated RNA N1‐methyladenosine (m1A) Demethylation
Zhang, L., Duan, H., Paduch, M., Hu, J., Zhang, C., Mu, Y., Lin, H., He, C., Kossiakoff, A. A., Jia, G., et al. (2023) · Angewandte Chemie · doi:10.1002/ange.202313900 · Cited by 1 · see citing works
Self-citationResearch progress of RNA modification and its association with human diseases
Gao, C., Guan, M., Xiao, H., Jin, H., Jin, Y., Liu, J., Luo, H., Qu, H., Xie, S., Yang, Y., et al. (2023) · Scientia Sinica Vitae · doi:10.1360/ssv-2023-0127
Lukinović, V., Hausmann, S., Roth, G. S., Oyeniran, C., Ahmad, T., Tsao, N., Brickner, J. R., Casanova, A. G., Chuffart, F., Benitez, A. M., et al. (2023) · doi:10.1158/2159-8290.c.6549634.v1
Self-citationMaimaiti, A., Baihetiyaer, Y., Turhon, M., Abulaiti, A., Cui, X., Pei, Y., Aili, Y., Aerken, D., Jiang, L., Wang, Y., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-2371294/v1
- Authors
- Tsao, N., Brickner, J. R., Rodell, R., Ganguly, A., Wood, M., Oyeniran, C., Ahmad, T., Sun, H., Bacolla, A., Zhang, L., Lukinović, V., Soll, J. M., Townley, B. A., Casanova, A. G., Tainer, J. A., He, C., Vindigni, A., Reynoird, N., & Mosammaparast, N.
- Affiliations
- Washington University in St. Louis (US)
- Centre National de la Recherche Scientifique (FR)
- The University of Texas MD Anderson Cancer Center (US)
- University of Chicago (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Mosammaparast, Nima
- ORCID
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2021-10
- Volume
- 81
- Issue
- 20
- Pages
- 4228-4242.e8
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC8931856
- OpenAlex
- W3205615234
- Cited by
- 46
- References
- 55
- Citations by year
- 2026: 7 · 2025: 12 · 2024: 7 · 2023: 11 · 2022: 8 · 2021: 1
- FWCI
- 2.12
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Rare & Special e-Zone (The Hong Kong University of Science and Technology) (submittedVersion)
- HAL (submittedVersion, other-oa)
- Funders
- National Institutes of Health
- US Department of Defense
- American Cancer Society
- Agence nationale de la recherche
- French National Cancer Institute
- National Science Foundation
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- RNA methylation, alkylation damage, ALKBH3, E3 ubiquitin ligase, R-loop formation, transcriptional repression, genotoxic stress response
- MeSH terms
- AlkB Homolog 3, Alpha-Ketoglutarate-Dependent Dioxygenase, R-Loop Structures, Cell Nucleus, DNA Helicases, DNA-Binding Proteins, HeLa Cells, Humans, Methylation, Neoplasms, Nuclear Proteins, RNA Processing, Post-Transcriptional, RNA, Neoplasm, Transcription, Genetic, Spliceosomes, DNA Methylation, Ubiquitination, HEK293 Cells
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